Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Changes to the Enzyme List concerning ATPases and GTPases

The entries below are additions and amendments to 'Enzyme Nomenclature' 1992 [Academic Press, San Diego, California, ISBN 0-12-227164-5 (hardback), 0-12-227165-3 (paperback)]. This has already been amended by supplements, obtainable at http://www.sbcs.qmul.ac.uk/iubmb/enzyme/ . The proposals below have been prepared for the NC-IUBMB by A. Kotyk, edited by Keith Tipton and Sinéad Boyce, and put onto the web by Gerry Moss. Comments and suggestions on enzyme classification and nomenclature may be sent to Professor K.F. Tipton (ktipton@tcd.ie) or Dr S. Boyce (sboyce@tcd.ie), Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland . These changes were approved at the meeting of NC-IUBMB held May 2000.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.

These entries replace EC 3.6.1.32 to EC 3.6.1.38; EC 3.6.1.32 is now EC 3.6.4.1, EC 3.6.1.33 is now EC 3.6.4.2, EC 3.6.1.34 is now EC 3.6.3.14, EC 3.6.1.35 is now EC 3.6.3.6, EC 3.6.1.36 is now EC 3.6.3.10, EC 3.6.1.37 is now EC 3.6.3.9 and EC 3.6.1.38 is now EC 3.6.3.8.

*EC 3.6.1.1

Recommended name: inorganic diphosphatase

Reaction: diphosphate + H2O = 2 phosphate

Systematic name: diphosphate phosphohydrolase

Comments: Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). A form of this enzyme with a molecular mass of about 90 kDa is found in tonoplasts of plants and fungi, where it imports protons from the cytosol into the vacuolar lumen.

References:

1. Bailey, K. and Webb, E.C. Purification and properties of yeast pyrophosphatase. Biochem. J. 38 (1944) 394-398.

2. Kunitz, M. Crystalline inorganic pyrophosphatase isolated from bakers' yeast. J. Gen. Physiol. 35 (1952) 423-450.

3. Rafter, G.W. Pyrophosphate metabolism in liver mitochondria. J. Biol. Chem. 235 (1960) 2475-2477.

*EC 3.6.1.5

Recommended name: apyrase

Reaction: ATP + 2 H2O = AMP + 2 phosphate

Other name(s): ATP-diphosphatase; adenosine diphosphatase; ADPase

Systematic name: ATP diphosphohydrolase

Comments: Requires Ca2+. Also acts on ADP, and on other nucleoside triphosphates and diphosphates. Most of the ecto-ATPases occurring on the cell surface and hydrolysing extracellular nucleoside triphosphates and diphosphates belong to this enzyme family. Either Ca2+ or Mg2+ can serve as activating ions.

References:

1. Krishnan, P.S. Apyrase, pyrophosphatase and metaphosphatase of Penecillium chrysogenum. Arch. Biochem. Biophys. 37 (1952) 224-234.

2. Liébecq, C., Lallemand, A. and Degueldre-Guillaume, M.-J. Partial purification and properties of potato apyrase. Bull. Soc. Chim. Biol. 45 (1963) 573-594.

3. Plaut, G.W.E. An inosine diphosphatase from mammalian liver. J. Biol. Chem. 217 (1955) 235-245.

3.6.1 In Phosphorus-Containing Anhydrides

EC 3.6.1.46

Recommended name: heterotrimeric G-protein GTPase

Reaction: GTP + H2O = GDP + orthophosphate

Systematic name: GTP phosphohydrolase (signalling)

Comments: This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and imhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different α subunits (39-52 kDa), 5 β subunits (36 kDa) and 12 γ subunits (6-9 kDa) are known.

References:

1. Neer, E.J. Heterotrimeric G proteins: organizers of transmembrane signals. Cell 80 (1995) 249-259. [Medline UI: 95136357]

2. Sprang, S.R. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66 (1997) 639-678. [Medline UI: 97386830]

3. Bondarenko, V.A., Deasi, M., Dua, S., Yamazaki, M., Amin, R.H., Yousif, K.K., Kinumi, T., Ohashi, M., Komori, N., Matsumoto, H., Jackson, K.W., Hayashi, F., Usukura, J., Lipikin, V.M. and Yamazaki, A. Residues within the polycationic region of cGMP phosphodiesterase γ subunit crucial for the interaction with transducin α subunit. Identification by endogenous ADP-ribosylation and site-directed mutagenesis. J. Biol. Chem. 272 (1997) 15856-15864. [Medline UI: 97332673]

4. Ming, D., Ruiz-Avila, L. and Margolskee, R.F. Characterization and solubilization of bitter-responsive receptors that couple to gustducin. Proc. Natl. Acad. Sci. USA 95 (1998) 8933-8938. [Medline UI: 98338019]

EC 3.6.1.47

Recommended name: small monomeric GTPase

Reaction: GTP + H2O = GDP + orthophosphate

Systematic name: GTP phosphohydrolase (cell-regulating)

Comments: A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the α-subunit of heterotrimeric G-protein GTPase (EC 3.6.1.46). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).

References:

1. Bourne, H.R., Sanders, D.A. and McCormick, F. The GTPase superfamily: conserved structure and molecular mechanisms. Nature 349 (1991) 117-127. [Medline UI: 91095015]

2. Hall, A. Small GTP-binding proteins and the regulation of actin cytoskeleton. Annu. Rev. Cell Biol. 10 (1994) 31-54. [Medline UI: 95194683]

3. Geyer, M. and Wittinghofer, A. GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins. Curr. Opin. Struct. Biol. 7 (1997) 786-792. [Medline UI: 98096525]

4. Vitale, N., Moss, J. and Vaughan, M. Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). J. Biol. Chem. 273 (1998) 2553-2560. [Medline UI: 98112795]

EC 3.6.1.48

Recommended name: protein-synthesizing GTPase

Reaction: GTP + H2O = GDP + orthophosphate

Other names: initiation factor (IF), elongation factor (EF), peptide-release or termination factor

Systematic name: GTP phosphohydrolase (mRNA-translation-assisting)

Comments: This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1α (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF1α catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.

References:

1. Kurzchalia, T.V., Bommer, U.A., Babkina, G.T. and Karpova, G.G. GTP interacts with the γ-subunit of eukaryotic initiation factor EIF-2. FEBS Lett. 175 (1984) 313-316. [Medline UI: 85004125]

2. Kisselev, L.L. and Frolova, L.Yu. Termination of translation in eukaryotes. Biochem. Cell Biol. 73 (1995) 1079-1086. [Medline UI: 96282712]

3. Rodnina, M.V., Savelsberg, A., Katunin, V.I. and Wintermeyer, W. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385 (1997) 37-41. [Medline UI: 97138218]

4. Freistroffer, D.V., Pavlov, M.Y., MacDougall, J., Buckingham, R.H. and Ehrenberg, M. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J. 16 (1997) 4126-4133. [Medline UI: 97138218]

5. Krab, I.M. and Parmeggiani, A. EF-Tu, a GTPase odyssey. Biochim. Biophys. Acta 1443 (1998) 1-22. [Medline UI: 99057580]

EC 3.6.1.49

Recommended name: signal-recognition-particle GTPase

Reaction: GTP + H2O = GDP + orthophosphate

Systematic name: GTP phosphohydrolase (protein-synthesis-assisting)

Comments: Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).

References:

1. Connolly, T. and Gilmore, R. The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide. Cell 57 (1989) 599-610. [Medline UI: 89249324]

2. Connolly, T., Rapiejko, P.J. and Gilmore, R. Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor. Science 252 (1991) 1171-1173. [Medline UI: 91233369]

3. Miller, J.D., Wilhelm, H., Gierasch, L., Gilmore, R. and Walter, P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366 (1993) 351-354. [Medline UI: 94067320]

4. Freymann, D.M., Keenan, R.J., Stroud, R.M. and Walter, P. Structure of the conserved GTPase domain of the signal recognition particle. Nature 385 (1997) 361-364. [Medline UI: 97156020]

EC 3.6.1.50

Recommended name: dynamin GTPase

Reaction: GTP + H2O = GDP + orthophosphate

Systematic name: GTP phosphohydrolase (vesicle-releasing)

Comments: An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.

References:

1. Warnock, D.E. and Schmid, S.L. Dynamin GTPase, a force-generating molecular switch. Bioessays 18 (1996) 885-893. [Medline UI: 97093504]

2. McClure, S.J. and Robinson, P.J. Dynamin, endocytosis and intracellular signalling. Mol. Membr. Biol. 13 (1996) 189-215. [Medline UI: 97167576]

3. Oh, P., McIntosh, D.P. and Schnitzer, J.E. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141 (1998) 101-114. [Medline UI: 98198470]

EC 3.6.1.51

Recommended name: tubulin GTPase

Reaction: GTP + H2O = GDP + orthophosphate

Systematic name: GTP phosphohydrolase (microtubule-releasing)

Comments: An intrinsic activity of α-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others.

References:

1. Yu, X.C. and Margolin, W. Ca2+-mediated GTP-dependent dynamic assembly of bacetrial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J. 16 (1997) 5455-5463 [Medline UI: 97459931]

2. Tian, G., Bhamidipati, A., Cowan, N.J . and Lewis, S.A. Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the α/β-tubulin heterodimer. J. Biol. Chem. 274 (1999) 24054-24058. [Medline UI: 99377038]

3. Roychowdhury, S., Panda, D., Wilson, L. and Rasenick, M.M. G protein α subunits activate tubulin GTPase and modulate microtubule polymerization dynamics. J. Biol. Chem. 274 (1999) 13485-13490. [Medline UI: 99240742]

EC 3.6.3 Acting on acid anhydrides; catalysing transmembrane movement of substances.

Several types of ATP phosphohydrolase are listed here. Entries EC 3.6.3.1 to EC 3.6.3.13 and EC 3.6.3.53 are enzymes undergoing covalent phosphorylation of an aspartate residue during the transport cycle; entries EC 3.6.3.14 and EC 3.6.3.15 refer to enzymes of complicated membrane and non-membrane location that can also serve in ATP synthesis; entry EC 3.6.3.16 is a multisubunit enzyme that is involved in arsenite transport only; entries EC 3.6.3.17 to EC 3.6.3.50 are two-domain enzymes of the ABC family; entries EC 3.6.3.51 and EC 3.6.3.52 are parts of a complex protein-transporting machinery in mitochondria and chloroplasts.

EC 3.6.3.1

Recommended name: Mg2+-ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Other name(s): flippase

Systematic name: ATP phosphohydrolase (phospholipid-flipping)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other ('flippase').

References:

1. Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823-832. [Medline UI: 94184211]

2. Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95-102. [Medline UI: 96436637]

3. Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429-10434. [Medline UI: 97256755]

EC 3.6.3.2

Recommended name: Mg2+-importing ATPase

Reaction: ATP + H2O + Mg2+out = ADP + orthophosphate + Mg2+in

Systematic name: ATP phosphohydrolase (Mg2+-importing)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in both Gram-positive and Gram-negative bacteria, and three types are known, designated as CorA, MgtA and MgtB. The major enzyme is CorA, which also transports Co2+ and Ni2+.

References:

1. Tao, T., Snavely, M.D., Farr, S.G. and Maguire, M.E. Magnesium transport in Salmonella typhimurium: mtgA encodes a P-type ATPase and is regulated by Mg2+ in a manner similar to that of the mgtB P-type ATPase. J. Bacteriol. 177 (1995) 2654-2662. [Medline UI: 95270580]

2. Smith, R.L., Szegedy, M.A., Kucharski, L.M., Walker, C., Wiet, R.M., Redpath, A., Kaczmarek, M.T. and Maguire, M.E. The CorA Mg2+ transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the third membrane domain identifies a Mg2+ pore. J. Biol. Chem. 273 (1998) 28663-28669. [Medline UI: 99003207]

EC 3.6.3.3

Recommended name: Cd2+-exporting ATPase

Reaction: ATP + H2O + Cd2+in = ADP + orthophosphate + Cd2+out

Systematic name: ATP phosphohydrolase (Cd2+-exporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants.

References:

1. Silver, S. and Ji, G. Newer systems for bacterial resistance to toxic heavy metals. Environ. Health Perspect. 102, Suppl. 3 (1994) 107-113. [Medline UI: 95145370]

2. Tsai, K.J. and Linet, A.L. Formation of a phosphorylated enzyme intermediate by the cadA Cd2+-ATPase. Arch. Biochem. Biophys. 305 (1993) 267-270. [Medline UI: 93384276]

EC 3.6.3.4

Recommended name: Cu2+-exporting ATPase

Reaction: ATP + H2O + Cu2+in = ADP + orthophosphate + Cu2+out

Systematic name: ATP phosphohydrolase (Cu2+-exporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This bacterial and mammalian enzyme exports Cu2+ from cells. In humans, it is involved in Menkes disease and Wilson's disease.

References:

1. Vulpe, C., Levinson, B., Whitney, S., Packman, S. and Gitschier, J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat. Genet. 3 (1993) 7-13. [Medline UI: 93258410]

2. Petrukhin, K., Lutsenko, S., Chernov, I., Ross, B.M., Kaplan, J.H. and Gilliam, T.C. Characterization of the Wilson disease gene encoding a P-type copper-transporting ATPase: genomic organization, alternative splicing, and structure/function predictions. Hum. Mol. Genet. 3 (1994) 1647-1656. [Medline UI: 95135423]

3. Fagan, M.J. and Saier, M.H., Jr. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 38 (1994) 57-99. [Medline UI: 94202222]

EC 3.6.3.5

Recommended name: Zn2+-exporting ATPase

Reaction: ATP + H2O + Zn2+in = ADP + orthophosphate + Zn2+out

Other name(s): Zn(II)-translocating P-type ATPase

Systematic name: ATP phosphohydrolase (Zn2+-exporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This bacterial and animal enzyme also exports Cd2+ and Pb2+.

References:

1. Oestreicher, P. and Cousins, R.J. Zinc uptake by basolateral membrane vesicles from rat small intestine. J. Nutr. 119 (1989) 639-646. [Medline UI: 89199133]

2. Rensing, C., Mitra, B. and Rosen, B.P. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc. Natl. Acad. Sci. USA 94 (1997) 14326-14331. [Medline UI: 98070750]

3. Rensing, C., Sun, Y., Mitra, B. and Rosen, B.P. Pb(II)-translocating P-type ATPases. J. Biol. Chem. 273 (1998) 32614-32617. [Medline UI: 99047637]

EC 3.6.3.6

Recommended name: H+-exporting ATPase

Reaction: ATP + H2O + H+in = ADP + orthophosphate + H+out

Other name(s): proton-translocating ATPase; yeast plasma membrane H+-ATPase; yeast plasma membrane ATPase

Systematic name: ATP phosphohydrolase (H+-exporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.

References:

1. Goffeau, A. and Slayman, C. The proton-translocating ATPase of the fungal plasma membrane. Biochim. Biophys. Acta 639 (1981) 197-223. [Medline UI: 82160888]

2. Serrano, R., Kielland-Brandt, M.C. and Fink, G.R. Yeast plasma membrane ATPase is essential for growth and has homology with (Na++K+)-, K+-and Ca2+-ATPases. Nature 319 (1986) 689-693. [Medline UI: 86146844]

3. Serrano, R. and Portillo, F. Catalytic and regulatory sites of yeast plasma membrane H+-ATPase studied by directed mutagenesis. Biochim. Biophys. Acta 1018 (1990) 195-199. [Medline UI: 90366582]

EC 3.6.3.7

Recommended name: Na+-exporting ATPase

Reaction: ATP + H2O + Na+in = ADP + orthophosphate + Na+out

Systematic name: ATP phosphohydrolase (Na+-exporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme, which is found in Gram-positive bacteria and in yeast, is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed.

References:

1. Wieland, J., Nitsche, A.M., Strayle, J., Steiner, H. and Rudolph, H.K. The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane. EMBO J. 14 (1995) 3870-3882. [Medline UI: 95393964]

2. Catty, P., de Kerchove d'Exaerde, A. and Goffeau, A. The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett. 409 (1997) 325-332. [Medline UI: 97367916]

3. Cheng, J., Guffanti, A.A. and Krulwich, T.A. A two-gene ABC-type transport system that extrudes Na+ in Bacillus subtilis is induced by ethanol or protonophore. Mol. Microbiol. 23 (1997) 1107-1120. [Medline UI: 97260108]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.8

Recommended name: Ca2+-transporting ATPase

Reaction: ATP + H2O + Ca2+cis = ADP + orthophosphate + Ca2+trans

Other name(s): sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca2+-ATPase

Systematic name: ATP phosphohydrolase (Ca2+-transporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in yeast. The first and third transport one ion per ATP hydrolysed, whereas the second transports two ions.

References:

1. Schatzmann, H.J. and Vicenzi, F.F. Calcium movements across the membrane of human red cells. J. Physiol. 201 (1969) 369-395. [Medline UI: 69166882]

2. Inesi, G., Watanabe, T., Coan, C. and Murphy, A. The mechanism of sarcoplasmic reticulum ATPase. Ann. NY Acad. Sci. 402 (1982) 515-532. [Medline UI: 83176731]

3. Carafoli, E. The Ca2+ pump of the plasma membrane. J. Biol. Chem. 267 (1992) 2115-2118. [Medline UI: 92129274]

4. MacLennan, D.H., Rice, W.J. and Green, N.M. The mechanism of Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases. J. Biol. Chem. 272 (1997) 28815-28818. [Medline UI: 98030547]

EC 3.6.3.9

Recommended name: Na+/K+-exchanging ATPase

Reaction: ATP + H2O + Na+in + K+out = ADP + orthophosphate + Na+out + K+in

Systematic name: ATP phosphohydrolase (Na+/K+-exchanging)

Other name: sodium pump; Na+,K+ pump

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na+ and influx of two K+ per ATP hydrolysed. It is apparently involved in generating the plasma membrane electrical potential.

References:

1. Skou, J.C. The influence of some cations on an adenosinetriphosphatase from peripheral nerve. Biochim. Biophys. Acta 23 (1957) 394-401.

2. Post, R.L., Sen, A.K. and Rosenthal, A.S. A phosphorylated intermediate in adenosine triphosphate-dependent sodium and potassium transport across kidney membrane. J. Biol. Chem. 240 (1965) 1437-1445.

3. Skou, J.C. The energy-coupled exchange of Na+ for K+ across the cell membrane. The Na+,K+ pump. FEBS Lett. 268 (1990) 314-324. [Medline UI: 90346185]

EC 3.6.3.10

Recommended name: H+/K+-exchanging ATPase

Reaction: ATP + H2O + H+in + K+out = ADP + orthophosphate + H+out + K+in

Other name(s): H+-K+-ATPase; H,K-ATPase

Systematic name: ATP phosphohydrolase (H+/K+-exchanging)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A gastric mucosal enzyme that catalyses the efflux of one H+ and the influx of one K+ per ATP hydrolysed.

References:

1. Sachs, G., Collier, R.H., Shoemaker, R.L. and Hirschowitz, B.I. The energy source for gastric H+ secretion. Biochim. Biophys. Acta 162 (1968) 210-219. [Medline UI: 69009790]

2. Hersey, S.J., Perez, A. Matheravidathu, S. and Sachs, G. Gastric H+-K+-ATPase in situ: evidence for compartmentalization. Am. J. Physiol. 257 (1989) G539-G547. [Medline UI: 90023875]

3. Rabon, E.C. and Reuben, M.A. The mechanism and structure of the gastric H,K-ATPase. Annu. Rev. Physiol. 52 (1990) 321-344. [Medline UI: 90233760]

EC 3.6.3.11

Recommended name: Cl--transporting ATPase

Reaction: ATP + H2O + Cl-out = ADP + orthophosphate + Cl-in

Other name(s): Cl--translocating ATPase; Cl--motive ATPase

Systematic name: ATP phosphohydrolase (Cl--importing)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. An animal and plant enzyme involved in the import of chloride anions.

References:

1. Ohhashi, T., Katsu, T. and Ikeda, M. Improvement of reconstitution of the Cl--translocating ATPase isolated from Acetabularia acetabulum into liposomes and several anion pump characteristics. Biochim. Biophys. Acta 1106 (1992) 165-170. [Medline UI: 92256441]

2. Gerencser, G.A. and Purushotham, K.R. Reconstituted Cl- pump protein: a novel Cl--motive ATPase. J. Bioenerget. Biomembr. 28 (1996) 459-469. [Medline UI: 97111576]

3. Inagaki, C., Hara, M. and Zeng, X.T. A Cl- pump in rat brain neurons. J. Exp. Zool. 275 (1996) 262-268. [Medline UI: 96327156]

EC 3.6.3.12

Recommended name: K+-transporting ATPase

Reaction: ATP + H2O + K+out = ADP + orthophosphate + K+in

Other name(s): K+-translocating Kdp-ATPase; multi-subunit K+-transport ATPase

Systematic name: ATP phosphohydrolase (K+-importing)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme of di(heterotetrameric) structure that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.

References:

1. Siebers, A. and Altendorf, K. Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli. J. Biol. Chem 264 (1989) 5831-5838. [Medline UI: 89174642]

2. Gassel, M., Siebers, A., Epstein, W. and Altendorf, K. Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli. Biochim. Biophys. Acta 1415 (1998) 77-84. [Medline UI: 99077600]

EC 3.6.3.13

Recommended name: aminophospholipid-transporting ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (aminophospholipid-transporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. An animal enzyme that is involved in the export of (amino)phospholipids and resembles a 'flippase' (see EC 3.6.3.1) in function.

References:

1. Zimmerman, M.L. and Daleke, D.L. Regulation of a candidate aminophospholipid-transporting ATPase by lipid. Biochemistry 32 (1993) 12257-12263. [Medline UI: 94032363]

2. Beleznay, Z., Zachowski, A., Devaux, P.F., Navazo, M.P. and Ott, P. ATP-dependent aminophospholipid translocation in erythrocyte vesicles: stoichiometry of transport. Biochemistry 32 (1993) 3146-3152. [Medline UI: 93208138]

3. Tang, X., Halleck, M.S., Schlegel, R.A. and Williamson, P. A subfamily of P-type ATPases with aminophospholipid-transporting activity. Science 272 (1996) 1495-1497. [Medline UI: 96234315]

EC 3.6.3.14

Recommended name: H+-transporting two-sector ATPase

Reaction: ATP + H2O + H+in = ADP + orthophosphate + H+out

Systematic name: ATP phosphohydrolase (H+-transporting)

Other names: ATP synthase; F1-ATPase; FoF1-ATPase

Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 α- and 3 β-subunits) is connected via the δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9-12 c subunits rotate by consecutive 120° angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archebacterial) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.

References:

1. Boyer, P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215-250. [Medline UI: 93112640]

2. Abrahams, J.P., Leslie, A.G.W., Lutter, R. and Walker, J.F. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 375 (1994) 621-628. [Medline UI: 94344236]

3. Blair, A., Ngo, L., Park, J., Paulsen, I.T. and Saier, M.H., Jr. Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the FoF1-ATPases of bacteria, chloroplasts and mitochondria. Microbiology 142 (1996) 17-32. [Medline UI: 96146047]

4. Noji, H., Yasuda, R., Yoshida, M. and Kinosita, K., Jr. Direct observation of the rotation of F1-ATPase. Nature 386 (1997) 299-302. [Medline UI: 97222141]

EC 3.6.3.15

Recommended name: Na+-transporting two-sector ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (Na+-transporting)

Other name: ATP synthase; vacuolar-type Na+-ATPase; Na+-translocating ATPase; Na+-translocating F1Fo-ATPase; vacuolar-type Na+-translocating ATPase

Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. An enzyme found in alkaliphilic bacteria that is similar to EC 3.6.3.14 (H+-transporting two-sector ATPase) where Na+ replaces H+.

References:

1. Solioz, M. and Davies, K. Operon of vacuolar-type Na+-ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 9453-9459. [Medline UI: 94193617]

2. Takase, K., Kakinuma, S., Yamato, I., Konishi, K., Igarashi, K. and Kanikuma, Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 11037-11044. [Medline UI: 94209269]

3. Rahlfs, S. and Müller, V. Sequence of subunit c of the Na+-translocating F1Fo-ATPase of Acetobacterium woodii: proposal for determinants of Na+ specificity as revealed by sequence comparisons. FEBS Lett. 404 (1997) 269-271. [Medline UI: 97227959]

EC 3.6.3.16

Recommended name: arsenite-transporting ATPase

Reaction: ATP + H2O + arsenitein = ADP + orthophosphate + arseniteout

Systematic name: ATP phosphohydrolase (arsenite-exporting)

Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. A bacterial enzyme that usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. Exports arsenite and antimonite anions.

References:

1. Silver, S., Misra, T.K. and Laddaga, R.A. DNA sequence analysis of bacterial toxic heavy metal resistance. Biol. Trace Elem. Res. 21 (1989) 145-163. [Medline UI: 91001290]

2. Rosen, B.P., Weigel, U., Monticello, R.A. and Edwards, B.P. Molecular analysis of an anion pump: purification of the ArsC protein. Arch. Biochem. Biophys. 284 (1991) 381-385. [Medline UI: 91112837]

3. Bruhn, D.F., Li, J., Silver, S., Roberto, F. and Rosen, B.P. The arsenical resistance operon of IncN plasmid R46. FEMS Microbiol. Lett. 139 (1996) 149-153. [Medline UI: 91112837]

4. Zhou, T., Rosen, B.P. and Gatti, D.L. Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 921-924. [Medline UI: 99190993]

EC 3.6.3.17

Recommended name: monosaccharide-transporting ATPase

Reaction: ATP + H2O + monosaccharideout = ADP + orthophosphate + monosaccharidein

Systematic name: ATP phosphohydrolase (monosaccharide-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside.

References:

1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [Medline UI: 93119750]

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Kemner, J.M., Liang, S. and Nester, E.W. The Agrobacterium tumefaciens virulence gene chvE is part of a putative ABC-type sugar transport operon. J. Bacteriol. 179 (1997) 2452-2458. [Medline UI: 97234664]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

5. Song, S. and Park, C. Utilization of D-ribose through D-xylose transporter. FEMS Microbiol. Lett. 163 (1998) 255-261. [Medline UI: 98336901]

6. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.18

Recommended name: oligosaccharide-transporting ATPase

Reaction: ATP + H2O + oligosaccharideout = ADP + orthophosphate + oligosaccharidein

Systematic name: ATP phosphohydrolase (disaccharide-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports lactose, melibiose and raffinose.

References:

1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [Medline UI: 93119750]

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Tam, R. and Saier, M.H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57 (1993) 320-346. [Medline UI: 93330183]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

5. Williams, S.G., Greenwood, J.A. and Jones, C.W. Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and β-galactosidase in Agrobacterium radiobacter. Mol. Microbiol. 6 (1992) 1755-1768. [Medline UI: 92334152]

EC 3.6.3.19

Recommended name: maltose-transporting ATPase

Reaction: ATP + H2O + maltoseout = ADP + orthophosphate + maltosein

Systematic name: ATP phosphohydrolase (maltose-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import maltose and maltose oligosaccharides.

References:

1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [Medline UI: 93119750]

2. Dassa, E. and Muir, S. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol. Microbiol. 7 (1993) 29-38. [Medline UI: 93172958]

3. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.20

Recommended name: glycerol-3-phosphate-transporting ATPase

Reaction: ATP + H2O + glycerol-3-phosphateout = ADP + orthophosphate + glycerol-3-phosphatein

Systematic name: ATP phosphohydrolase (glycerol-3-phosphate-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphorylated glycerol.

References:

1. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

2. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

3. Bahl, H., Burchhardt, G. and Wienecke, A. Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes homologous to Escherichia coli genes encoding integral membrane components of binding-protein-dependent transport systems. FEMS Microbiol. Lett. 65 (1991) 83-87. [Medline UI: 91340095]

EC 3.6.3.21

Recommended name: polar-amino-acid-transporting ATPase

Reaction: ATP + H2O + polar amino acidout = ADP + orthophosphate + polar amino acidin

Other name(s): histidine permease

Systematic name: ATP phosphohydrolase (polar-amino-acid-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

3. Nikaido, K., Liu, P.Q. and Ferro-Luzzi Ames, G. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubilization, dimerization , and ATPase activity. J. Biol. Chem. 272 (1997) 27745-27752. [Medline UI: 98010611]

4. Walshaw, D.L., Lowthorpe, S., East, A. and Poole, P.S. Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity. FEBS Lett. 414 (1997) 397-401. [Medline UI: 97459767]

EC 3.6.3.22

Recommended name: nonpolar-amino-acid-transporting ATPase

Reaction: ATP + H2O + nonpolar amino acidout = ADP + orthophosphate + nonpolar amino acidin

Systematic name: ATP phosphohydrolase (nonpolar-amino-acid-transporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import Leu, Ile and Val.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.23

Recommended name: oligopeptide-transporting ATPase

Reaction: ATP + H2O + oligopeptideout = ADP + orthophosphate + oligopeptidein

Other name(s): oligopeptide permease

Systematic name: ATP phosphohydrolase (oligopeptide-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports di- and oligopeptides.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

4. Pearce, S.R., Mimmack, M.L., Gallagher, M.P., Gileadi, U., Hyde, S.C. and Higgins, C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 6 (1992) 47-57. [Medline UI: 92149312]

EC 3.6.3.24

Recommended name: nickel-transporting ATPase

Reaction: ATP + H2O + Ni2+out = ADP + orthophosphate + Ni2+in

Systematic name: ATP phosphohydrolase (nickel-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Ni2+.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Hendricks, J.K. and Mobley, H.L. Helicobacter pylori ABC transporter: effect of allelic exchange murtagenesis on urease activity. J. Bacteriol. 179 (1997) 5892-5902. [Medline UI: 97440142]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.25

Recommended name: sulfate-transporting ATPase

Reaction: ATP + H2O + sulfateout = ADP + orthophosphate + sulfatein

Systematic name: ATP phosphohydrolase (sulfate-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports sulfate and thiosulfate anions.

References:

1. Sirko, A., Zatyka, M., Sadowy, E. and Hulanicka, D. Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins. J. Bacteriol. 177 (1995) 4134-4136. [Medline UI: 95332222]

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.26

Recommended name: nitrate-transporting ATPase

Reaction: ATP + H2O + nitrateout = ADP + orthophosphate + nitratein

Systematic name: ATP phosphohydrolase (nitrate-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports NO3-, NO2- and OCN-.

References:

1. Omata, T. Structure, function and regulation of the nitrate transport system of the cyanobacterium Synechococcus sp. PCC7942. Plant Cell Physiol. 36 (1995) 207-213.

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.27

Recommended name: phosphate-transporting ATPase

Reaction: ATP + H2O + phosphateout = ADP + orthophosphate + phosphatein

Other name(s): ABC phosphate transporter

Systematic name: ATP phosphohydrolase (phosphate-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphate anions.

References:

1. Webb, D.C., Rosenberg, H. and Cox, G.B. Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. A role for proline residues in transmembrane helices. J. Biol. Chem. 267 (1992) 24661-24668. [Medline UI: 93077562]

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Braibant, M., LeFevre, P., de Wit, L., Ooms, J., Peirs, P., Huygen, K., Wattiez, R. and Content, J. Identification of a second Mycobacterium tuberculosis gene cluster encoding proteins of an ABC phosphate transporter. FEBS Lett. 394 (1996) 206-212. [Medline UI: 97000022]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.28

Recommended name: phosphonate-transporting ATPase

Reaction: ATP + H2O + phosphonateout = ADP + orthophosphate + phosphonatein

Systematic name: ATP phosphohydrolase (phosphonate-transporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphonate and organophosphate anions.

References:

1. Wanner, B.L. and Metcalf, W.W. Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation. FEMS Microbiol. Lett. 79 (1992) 133-139. [Medline UI: 93122525]

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.29

Recommended name: molybdate-transporting ATPase

Reaction: ATP + H2O + molybdateout = ADP + orthophosphate + molybdatein

Systematic name: ATP phosphohydrolase (molybdate-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports molybdate anions.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Grunden, A.M. and Shanmugam, K.T. Molybdate transport and regulation in bacteria. Arch. Mikrobiol. 168 (1997) 345-354. [Medline UI: 98004559]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.30

Recommended name: Fe3+-transporting ATPase

Reaction: ATP + H2O + Fe3+out = ADP + orthophosphate + Fe3+in

Systematic name: ATP phosphohydrolase (ferric-ion-transporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports ferric cations.

References:

1. Angerer, A., Klupp, B. and Braun, V. Iron transport systems of Serratia marcescens. J. Bacteriol. 174 (1992) 1378-1387. [Medline UI: 92138634]

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

4. Khun, H.H., Kirby, S.D. and Lee, B.C. A Neisseria meningitidis fbp ABC mutant is incapable of using nonheme iron for growth. Infect. Immun. 66 (1998) 2330-2336. [Medline UI: 98234069]

EC 3.6.3.31

Recommended name: polyamine-transporting ATPase

Reaction: ATP + H2O + polyamineout = ADP + orthophosphate + polyaminein

Systematic name: ATP phosphohydrolase (polyamine-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine.

References:

1. Kashiwagi, K., Miyamoto, S., Nukui, E., Kobayashi, H. and Igarashi, K. Functions of potA and potD proteins in spermidine - preferential uptake system in Escherichia coli. J. Biol. Chem. 268 (1993) 19358-19363. [Medline UI: 93374918]

2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.32

Recommended name: quaternary-amine-transporting ATPase

Reaction: ATP + H2O + quaternary amineout = ADP + orthophosphate + quaternary aminein

Systematic name: ATP phosphohydrolase (quaternary-amine-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports betaine and glycine.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Kempf, B., Gade, J. and Bremer, E. Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant. J. Bacteriol. 179 (1997) 6213-6220. [Medline UI: 97474241]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.33

Recommended name: vitamin B12-transporting ATPase

Reaction: ATP + H2O + vitamin B12out = ADP + orthophosphate + vitamin B12in

Systematic name: ATP phosphohydrolase (vitamin B12-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports cobalamin derivatives.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

3. Friedrich, M.J., de Veaux, L.C. and Kadner, R.J. Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems. J. Bacteriol. 167 (1986) 928-934. [Medline UI: 86304184]

EC 3.6.3.34

Recommended name: iron-chelate-transporting ATPase

Reaction: ATP + H2O + iron chelateout = ADP + orthophosphate + iron chelatein

Systematic name: ATP phosphohydrolase (iron-chelate-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Fe-enterobactin, Fe-dicitrate, Fe-hydroxamate and other siderophores.

References:

1. Shea, C.M. and McIntosh, M.A. Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding-protein-dependent systems in Escherichia coli. Mol. Microbiol. 5 (1991) 1415-1428. [Medline UI: 92157868]

2. Koster, W. and Böhm, B. Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport. Mol. Gen. Genet. 232 (1992) 399-407. [Medline UI: 92269759]

3. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

5. Mademidis, A. and Koster, W. Transport activity of FhuA, FhuC, FhuD and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake. Mol. Gen. Genet. 258 (1998) 156-165. [Medline UI: 98273640]

EC 3.6.3.35

Recommended name: manganese-transporting ATPase

Reaction: ATP + H2O + Mn2+out = ADP + orthophosphate + Mn2+in

Other name(s): ABC-type manganese permease complex

Systematic name: ATP phosphohydrolase (manganese-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Mn2+, Zn2+ and iron chelates.

References:

1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [Medline UI: 96008865]

2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

3. Novak, R., Braun, J.S., Charpentier, E. and Tuomanen, E. Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa. Mol. Microbiol. 29 (1998) 1285-1296. [Medline UI: 98449534]

4. Kolenbrander, P.E., Andersen, R.N., Baker, R.A. and Jenkinson, H.F. The adhesion-assoiated aca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn2+ uptake. J. Bacteriol. 180 (1998) 290-295. [Medline UI: 98101468]

EC 3.6.3.36

Recommended name: taurine-transporting ATPase

Reaction: ATP + H2O + taurineout = ADP + orthophosphate + taurinein

Systematic name: ATP phosphohydrolase (taurine-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports taurine.

References:

1. van der Ploeg, J.R., Weiss, M.A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M.A. and Leisinger, T. Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178 (1996) 5438-5446. [Medline UI: 96404792]

EC 3.6.3.37

Recommended name: guanine-transporting ATPase

Reaction: ATP + H2O + guanineout = ADP + orthophosphate + guaninein

Systematic name: ATP phosphohydrolase (guanine-importing)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A eukaryotic enzyme that imports guanine and tryptophan (it contains a single ATP-binding site).

References:

1. Dreesen, T.D., Johnson, D.H and Henikoff, S. The brown protein of Drosophila melanogaster is similar to the white protein and to components of active transport complexes. Mol. Cell Biol. 8 (1988) 5206-5215. [Medline UI: 89218981]

2. Tearle, R.G., Belote, J.M., McKeown, M., Baker, B.S. and Howells, A.J. Cloning and characterization of the scarlet gene of Drosophila melanogaster. Genetics 122 (1989) 595-606. [Medline UI: 89339145]

3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.38

Recommended name: capsular-polysaccharide-transporting ATPase

Reaction: ATP + H2O + capsular polysaccharidein= ADP + orthophosphate + capsular polysaccharideout

Systematic name: ATP phosphohydrolase (capsular-polysaccharide-exporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme that exports capsular polysaccharide from Gram-negative bacteria.

References:

1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [Medline UI: 94133968]

2. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [Medline UI: 97419507]

3. Pigeon, R.P. and Silver, R.P. Analysis of the G93E mutant allele of KpsM, the membrane component of an ABC transporter involved in polysialic acid translocation in Escherichia coli K1.FEMS. Microbiol. Lett. 156 (1997) 217-222. [Medline UI: 98174453]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.39

Recommended name: lipopolysaccharide-transporting ATPase

Reaction: ATP + H2O + lipopolysaccharidein = ADP + orthophosphate + lipopolysaccharideout

Systematic name: ATP phosphohydrolase (lipopolysaccharide-exporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Enzymes of Gram-negative bacteria that export lipo-oligosaccharides and lipopolysaccharides.

References:

1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [Medline UI: 94133968]

2. Fernandez-Lopez, M., D'Haeze, W., Mergaert, P., Verplancke, C., Prome, J.C., Van Montagu, M. and Holstens, M. Role of nod1and nodJ in lipo-chitooligosaccharide secretion in Azorhizobium caulinodans and Escherichia coli. Mol. Microbiol. 20 (1996) 993-1000. [Medline UI: 96405623]

3. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [Medline UI: 97419507]

4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.40

Recommended name: teichoic-acid-transporting ATPase

Reaction: ATP + H2O + teichoic acidin = ADP + orthophosphate + teichoic acidout

Systematic name: ATP phosphohydrolase (teichoic-acid-exporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-positive bacteria that exports teichoic acid.

References:

1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [Medline UI: 94133968]

2. Lazarevic, V. and Karamoto, D. The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids. Mol. Microbiol. 16 (1995) 345-355. [Medline UI: 96015447]

3. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [Medline UI: 97419507]

4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.41

Recommended name: heme-transporting ATPase

Reaction: ATP + H2O + hemein = ADP + orthophosphate + hemeout

Systematic name: ATP phosphohydrolase (heme-exporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-negative bacteria that exports heme.

References:

1. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

2. Jekabsons, W. and Schuster, W. orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria. Mol. Gen. Genet. 246 (1995) 166-173. [Medline UI: 95166173]

3. Ramseier, T.M., Winteler, H.V. and Hennecke, H. Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes. J. Biol. Chem. 266 (1991) 7793-7803. [Medline UI: 91210304]

EC 3.6.3.42

Recommended name: β-glucan-transporting ATPase

Reaction: ATP + H2O + β-glucanin = ADP + orthophosphate + β-glucanout

Systematic name: ATP phosphohydrolase (β-glucan-exporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-negative bacteria that exports β-glucan.

References:

1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [Medline UI: 94133968]

2. Becker, A., Kuster, H., Niehaus, K. and Puhler, A. Extension of the Rhizobium meliloti succinoglycan biosynthesis gene cluster: identification of the exsA gene encoding an ABC transporter protein, and the exsB gene which probably codes for a regulator of succinoglycan biosynthesis. Mol. Gen. Genet. 249 (1995) 487-497. [Medline UI: 96133689]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.43

Recommended name: peptide-transporting ATPase

Reaction: ATP + H2O + peptidein = ADP + orthophosphate + peptideout

Systematic name: ATP phosphohydrolase (peptide-exporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A family of enzymes that exports α-hemolysin, cyclolysin, colicin V and siderophores from Gram-negative bacteria, and bacteriocin, subtilin, competence factor and pediocin from Gram-positive bacteria.

References:

1. Klein, C. and Entian, K.D. Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633. Appl. Environ. Microbiol. 60. (1994) 2793-2801. [Medline UI: 94368094]

2. Momburg, F., Roelse, J., Howard, J.C., Butcher, G.W., Hammerling, G.J. and Neefjes, J.J. Selectivity of MHC-encoded peptide transporters from human, mouse and rat. Nature 367 (1994) 648-651. [Medline UI: 94150681]

3. Binet, R., Létoffé, S., Ghigo, J.M., Delepaire, P. and Wanderman, C. Protein secretion by Gram-negative bacterial ABC exporters - a review. Gene 192 (1997) 7-11. [Medline UI: 97368101]

EC 3.6.3.44

Recommended name: xenobiotic-transporting ATPase

Reaction: ATP + H2O + xenobioticin = ADP + orthophosphate + xenobioticout

Systematic name: ATP phosphohydrolase (xenobiotic-exporting)

Other names: multidrug-resistance protein, P-glycoprotein

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Enzymes of Gram-positive bacteria and eukaryotic cells that export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them transport glutathione conjugates with drugs. Some also show some 'flippase' (Mg2+-ATPase; EC 3.6.3.1) activity.

References:

1. Bellamy, W.T. P-glycoproteins and multidrug resistance.Annu. Rev. Pharmac. Toxicol. 36 (1996) 161-183. [Medline UI: 96293306]

2. Frijters. C.M., Ottenhoff, R., Van Wijland, M.J., Van Nieuwkerk, C., Groen, A.K. and Oude-Elferink, R.P. Influence of bile salts on hepatic mdr2 P-glycoprotein expression. Adv. Enzym. Regul. 36 (1996) 351-363. [Medline UI: 97023395]

3. Keppler, D., König, J. and Buchler, M. The canalicular multidrug resistance protein, cMRP/MRP2, a novel conjugate export pump expressed in the apical membrane of hepatocytes. Adv. Enzyme Regul. 37 (1997) 321-333. [Medline UI: 98020949]

4. Loe, D.W., Deeley, R.G. and Cole, S.P. Characterization of vincristine transport by the Mr 190 000 multidrug resistance protein (MRP): evidence for cotransport with reduced glutathione. Cancer Res. 58 (1998) 5130-5136. [Medline UI: 99040657]

5. van Veen, H.W. and Konings, W.N. The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta 1365 (1998) 31-36. [Medline UI: 98358589]

6. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

EC 3.6.3.45

Recommended name: steroid-transporting ATPase

Reaction: ATP + H2O + steroidin = ADP + orthophosphate + steroidout

Systematic name: ATP phosphohydrolase (steroid-exporting)

Other name: pleiotropic-drug-resistance protein; PDR protein

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast protein that exports a variety of xenobiotics, especially steroids.

References:

1. Prasad, R., De Wergifosse, P., Goffeau, A. and Balzi, E. Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals. Curr. Genet. 27 (1995) 320-329. [Medline UI: 95339406]

2. Nagao, K., Taguchi, Y., Arioka, M., Kadokura, H., Takatsuki, A., Yoda, K. and Yamasaki, M. bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily. J. Bacteriol. 177 (1995) 1536-1543. [Medline UI: 95189731]

3. Mahé, Y., Lemoine, Y. and Kuchler, K. The ATP-binding cassette transporters Pdr5 and Snq2 of Saccharomyces cerevisiae can mediate transport of steroids in vivo J. Biol. Chem. 271 (1996) 25167-25172. [Medline UI: 96411720]

EC 3.6.3.46

Recommended name: cadmium-transporting ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (heavy-metal-exporting)

Other name: yeast cadmium factor

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole.

References:

1. Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509-6517. [Medline UI: 96198121]

2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.47

Recommended name: fatty-acyl-CoA-transporting ATPase

Reaction: ATP + H2O + fatty acyl CoAcis = ADP + orthophosphate + fatty acyl Cotrans

Systematic name: ATP phosphohydrolase (fatty-acyl-CoA-transporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.

References:

1. Kamijo, K., Taketani, S., Yokota, S., Osumi, T. and Hashimoto, T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glcoprotein)-related ATP-binding protein superfamily. J. Biol. Chem. 265 (1990) 4534-4540. [Medline UI: 90170961]

2. Hettema, E.H., van Roermund, C.W.T., Distel, B., van den Berg. M., Vilela, C., Rodrigues-Posada, C., Wanders, R.J.A. and Tabak, H.F. The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. EMBO J. 15 (1996) 3813-3822. [Medline UI: 96324389]

3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.48

Recommended name: α-factor-transporting ATPase

Reaction: ATP + H2O + α-factorin = ADP + orthophosphate + α-factorout

Systematic name: ATP phosphohydrolase (α-factor-transporting)

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports the α-factor sex pheromone.

References:

1. Michaelis, S. STE6, the yeast α-factor exporter. Semin. Cell Biol. 4 (1993) 17-27. [Medline UI: 93200459]

2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [Medline UI: 99106651]

EC 3.6.3.49

Recommended name: channel-conductance-controlling ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (channel-conductance-controlling)

Other name: cystic-fibrosis membrane-conductance-regulating protein

Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An animal enzyme that is active in forming a chloride channel, the absence of which brings about cystic fibrosis. It is also involved in the functioning of other transmembrane channels.

References:

1. Chen, M. and Zhang, J.T. Membrane insertion, processing, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes. Mol. Membr. Biol. 13 (1996) 33-40. [Medline UI: 97012581]

2. Tusnady, G.E., Bakos, E., Varadi, A. and Sarkadi, B. Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters. FEBS Lett. 402 (1997) 1-3. [Medline UI: 97165952]

3. Sheppard, D.N. and Welsh, M.J. Structure and function of the CFTR chloride channel. Physiol. Rev. 79 (1999) S23-S45. [Medline UI: 99126612]

EC 3.6.3.50

Recommended name: protein-secreting ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (protein-secreting)

Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. There are several families of enzymes included here, e.g. ATP-hydrolysing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eucarya,whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.

References:

1. Saier, M.H., Jr., Tam. R., Reizer, A. and Reizer, J. Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol. Microbiol. 11 (1994) 841-847. [Medline UI: 94293757]

2. Mecsas, J. and Strauss, E.J. Molecular mechanisms of bacterial virulence: type III secretion and pathogenicity islands. Emerg. Infect. Diseases. 2 (1996) 270-288. [Medline UI: 97125927]

3. Thomas, J.D., Reeves, P.J. and Salmond, G.P. The general secretion pathway of Erwinia carotovora subsp. carotovora: analysis of the membrane topology of OutC and OutF. Microbiology 143 (1997) 713-720. [Medline UI: 97237703]

4. Baker, B., Zambryski, P., Staskawicz, B. and Dinesh-Kumar, S.P. Signaling in plant-microbe interactions. Science 276 (1997) 726-733. [Medline UI: 97277211]

5. Martinez, A., Ostrovsky, P. and Nunn, D.N. Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion. Mol. Microbiol. 28 (1998) 1235-1246. [Medline UI: 98343806]

6. Schuch, R. and Maurelli, A.T. The mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasin translocation. Infect. Immun. 67 (1999) 1982-1991. [Medline UI: 99185030]

EC 3.6.3.51

Recommended name: mitochondrial protein-transporting ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (mitochondrial protein-importing)

Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex. (TIM is the protein transport machinery of the inner mitochondrial membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.)

References:

1. Bomer, U., Meijer, M., Maarse, A.C., Honlinger, A., Dekker, P.J., Pfanner, N. and Rassow, J. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane. EMBO J. 16 (1997) 2205-2216. [Medline UI: 97315162]

2. Berthold, J., Bauer, M.F., Schneider, H.C., Klaus, C., Dietmeier, K., Neupert, W. and Brunner, M. The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP-driving system. Cell 81 (1995) 1085-1093. [Medline UI: 95323964]

3. Voos, W., Martin, H., Krimmer, T. and Pfanner, N. Mechanisms of protein translocation into mitochondria. Biochim. Biophys. Acta 1422 (1999) 235-254. [Medline UI: 20018045]

EC 3.6.3.52

Recommended name: chloroplast protein-transporting ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (chloroplast protein-importing)

Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).

References:

1. Cline, K., Ettinger, N.F. and Theg, S.M. Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J. Biol. Chem. 267 (1992) 2688-2696. [Medline UI: 92129361]

2. Nakai, M., Goto, A., Nohara, T., Sugito, D. and Endo, T. Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J. Biol. Chem. 269 (1994) 31338-33341. [Medline UI: 95081065]

3. Scott, S.V. and Theg, S.M. A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implications. J. Cell Biol. 132 (1996) 63-75. [Medline UI: 96149457]

EC 3.6.3.53

Recommended name: Ag+-exporting ATPase

Reaction: ATP + H2O + Ag+in = ADP + orthophosphate + Ag+out

Systematic name: ATP phosphohydrolase (Ag+-exporting)

Comments: A P-type ATPase that exports Ag+ ions from pathogenic microorganisms as well as from some animal tissues.

References:

1. Gupta, A., Matsui, K., Lo, J.F. and Silver, S. Molecular basis for resistance to silver cations in Salmonella. Nature Med. 5 (1999) 183-188. [Medline UI: 99128056]

2. Bury, N.R., Grosell, M., Grover, A.K. and Wood, C.M. ATP-dependent silver transport across the basolateral membrane of rainbow trout gills. Toxicol. Appl. Pharmacol. 159 (1999) 1-8. [Medline UI: 99380675]

EC 3.6.4 Acting on acid anhydrides; involved in cellular and subcellular movement.

EC 3.6.4.1

Recommended name: myosin ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Other name: actomyosin

Systematic name: ATP phosphohydrolase (actin-translocating)

Comments: Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.

References:

1. Rayment, I. The structural basis of myosin ATPase activity. J. Biol. Chem. 271 (1996) 15850-15853. [Medline UI: 96279116]

2. Hasson, T. and Mooseker, M.S. Vertebrate unconventional myosins. J. Biol. Chem. 271 (1996) 16431-16434. [Medline UI: 96279199]

3. Murphy, C.T. and Spudich, J.A. The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity. Biochemistry 38 (1999) 3785-3792. [Medline UI: 99192418]

EC 3.6.4.2

Recommended name: dynein ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (tubulin-translocating)

Comments: A multisubunit protein complex associated with microtubules. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome towards the microtubule's minus end. It also functions in the movement of eukaryotic flagella and cilia. It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa).

References:

1. Summers, K.E. and Gibbons, I.R. Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm. Proc. Natl. Acad. Sci. USA 68 (1971) 3092-3096. [Medline UI: 72075180]

2. Gibbons, I.R. Dynein ATPases as microtubule motors. J. Biol. Chem. 263 (1988) 15837-15840. [Medline UI: 89034027]

3. Gee, M. and Vallee, R. The role of the dynein stalk in cytoplasmic and flagellar motility. Eur. Biophys. J. 27 (1998) 466-473. [Medline UI: 98433437]

EC 3.6.4.3

Recommended name: microtubule-severing ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (tubulin-dimerizing)

Other name: katanin

Comments: Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.

References:

1. McNally, F.J. and Vale, R.D. Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 75 (1993) 419-429. [Medline UI: 94037090]

2. Hartman, J.J., Mahr, J., McNally, K., Okawa, K., Iwamatsu, A., Thomas, S., Cheesman, S., Heuser, J., Vale, R.D. and McNally, F.J. Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit. Cell 93 (1998) 277-287. [Medline UI: 98227670]

EC 3.6.4.4

Recommended name: plus-end-directed kinesin ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Other name(s): kinesin

Systematic name: kinesin ATP phosphohydrolase (plus-end-directed)

Comments: Microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (α) chains (110 kDa) and two or more light (β) chains (65-75 kDa). Also hydrolyses GTP.

References:

1. Vale, R.D., Reese, T.S. and Sheetz, M.P. Identification of a novel force-generating protein, kinesin, in microtubule-based motility. Cell 42 (1985) 39-50. [Medline UI: 85254940]

2. Howard, J. Molecular motors: structural adaptations to cellular functions. Nature 389 (1997) 561-567. [Medline UI: 97474470]

3. Nakagawa, T., Tanaka, Y., Matsuoka, E., Kondo, S., Okada, Y., Noda, F., Kanai, Y. and Hirokawa, N. Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome. Proc. Natl. Acad. Sci. USA 94 (1997) 9654-9659. [Medline UI: 97420736]

EC 3.6.4.5

Recommended name: minus-end-directed kinesin ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: kinesin ATP phosphohydrolase (minus-end-directed)

Comments: Structurally almost identical to EC 3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules.

References:

1. Henningsen, U. and Schliwa, M. Reversal in the direction of movement of a molecular motor. Nature 389 (1997) 93-96. [Medline UI: 97433334]

2. Sharp, D.J., Kuriyama, R., Essner, R. and Baas, P.W. Expression of a minus-end-directed motor protein induces Sh9 cells to form axon-like processes with uniform microtubule polarity orientation. J. Cell Sci. 110 (1997) 2373-2380. [Medline UI: 98008416]

3. Sablin, E.P., Case, R.B., Dai, S.C., Hart, C.L., Ruby, A., Vale, R.D. and Fletterick, R.J. Direction determination in the minus-end-directed kinesin motor ncd. Nature 395 (1998) 813-816. [Medline UI: 99010841]

EC 3.6.4.6

Recommended name: vesicle-fusing ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (vesicle-fusing)

Comments: A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome.

References:

1. Confalonieri, F. and Duguet, M. A 200-amino acid ATPase module in search of a basic function. BioEssays 17 (1995) 639-650. [Medline UI: 95374488]

2. Imamura, A., Tamura, S., Shimoyawa, N., Suzuki, Y., Zhang, Z., Tsukamoto, T., Orii, T., Kondo, N., Osumi, T. and Fujiki, Y. Temperature-sensitive mutation in PEX1 moderates the phenotypes of peroxisome deficiency disorders. Hum. Mol. Genet. 7 (1998) 2089-2094. [Medline UI: 99036679]

3. Babst, W., Wendland, B., Estepa, E.J. and Emr, S.D. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17 (1998) 2982-2983. [Medline UI: 98270865]

EC 3.6.4.7

Recommended name: peroxisome-assembly ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Other name(s): peroxisome assembly factor-2

Systematic name: ATP phosphohydrolase (peroxisome-assembling)

Comments: An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa.

References:

1. Lee, Y.J. and Wickner, R.B. AFG1, a new member of the SEC18-NSF, PAS1, CDC48-VCP, TBP family of ATPases. Yeast 8 (1992) 787-790. [Medline UI: 93070616]

2. Tsukamoto,T., Miura, S., Nakai, T., Yokota, S., Shimozawa, N., Suzuki, Y., Orii, T., Fujiki, Y., Sakai, F., Bogaki, A., Yasumo, H. and Osumi, T. Peroxisome assembly factor-2, a putative ATPase cloned by functional complementation on a peroxisome-deficient mammalian cell mutant. Nat. Genet. 11 (1995) 395-401. [Medline UI: 96083586]

3. Yahraus, T., Braverman, N., Dodt, G., Kalish, J.E., Morrell, J.C., Moser, H.W., Valle, D. and Gould, S.J. The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor. EMBO J. 15 (1996) 2914-2923. [Medline UI: 96272151]

EC 3.6.4.8

Recommended name: proteasome ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (polypeptide-degrading)

Other name: RP triple-A protein; RP triphosphatase

Comments: Belongs to the AAA-type superfamily and, like EC 3.6.4.5 (minus-end-directed kinesin ATPase), is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.

References:

1. Rivett, A.J., Mason, G.G., Murray, R.Z. and Reidlinger, J. Regulation of proteasome structure and function. Mol. Biol. Rep. 24 (1997) 99-102. [Medline UI: 97372025]

2. Mason, G.G., Murray, R.Z., Pappin, D. and Rivett, A.J. Phosphorylation of ATPase subunits of the 26S proteasome. FEBS Lett. 430 (1998) 269-274. [Medline UI: 98351839]

EC 3.6.4.9

Recommended name: chaperonin ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Other name(s): chaperonin

Systematic name: ATP phosphohydrolase (polypeptide-unfolding)

Comments: Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or to entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 3.6.4.8 (proteasome ATPase).

References:

1. Hemmingsen, S.M., Woolford, C., van der Vies, S.M., Tilly, K., Dennis, D.T., Georgopoulos, G.C., Hendrix, R.W. and Ellis, R.J. Homologous plant and bacterial proteins: chaperone oligomeric protein assembly. Nature 333 (1988) 330-334. [Medline UI: 88232881]

2. Lubber, T.H., Donaldson, G.K., Viitanen, P.V. and Gatenby, A.A. Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone. Plant Cell 1 (1989) 1223-1230.

3. Ellis, R.J. (Ed.), The Chaperonins, Academic Press, San Diego, 1996.

4. Ranson, N.A., White, H.E. and Saibil, H.R. Chaperonins. Biochem. J. 333 (1998) 233-242. [Medline UI: 98324881]

EC 3.6.4.10

Recommended name: non-chaperonin molecular chaperone ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Other name(s): molecular chaperone Hsc70 ATPase

Systematic name: ATP phosphohydrolase (polypeptide-polymerizing)

Comments: This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.

References:

1. Sadis, S. and Hightower, L.E. Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31 (1992) 9406-9412. [Medline UI: 93003090]

2. Blond-Elquindi, S., Fourie, A.M., Sambrook, J.F. and Gething, M.J. Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J. Biol. Chem. 268 (1993) 12730-12735. [Medline UI: 93286116]

3. Wawrzynow, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Jonsen, M., Graves, B., Georgopoulos, C. and Zylicz, M. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14 (1995) 1867-1877. [Medline UI: 95262627]

4. Sriram, M., Osipiuk, J., Freeman, B., Morimoto, R. and Joachimiak, A. Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure 5 (1997) 403-414. [Medline UI: 97238936]

5. Li, X., Su, R.T., Hsu, H.T. and Sze, H. The molecular chaperone calnexin associated with the vacuolar H+-ATPase from oat seedlings. Plant Cell 10 (1998) 119-130. [Medline UI: 98138062]

EC 3.6.4.11

Recommended name: nucleoplasmin ATPase

Reaction: ATP + H2O = ADP + orthophosphate

Systematic name: ATP phosphohydrolase (nucleosome-assembling)

Comments: An acidic nuclear protein that is active in the ATP-dependent assembly of nucleosome cores, in decondensation of sperm chromatin and in other histone-involving processes.

References:

1. Laskey, R.A., Mills, A.D., Philpott, A., Leno, G.H., Dilworth, S.M. and Dingwall, C. The role of nucleoplasmin in chromatin assembly and disassembly. Phil. Trans. R. Soc. London B Biol. Sci. 339 (1993) 263-269. [Medline UI: 93262064]

2. Cote, J., Quinn, J., Workman, J.L. and Peterson, C.L. Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex. Science 265 (1994) 53-60. [Medline UI: 94287202]

3. Ito, T., Tyler, J.K., Bulger, M., Kobayashi, R. and Kadonaga, J.T. ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster. J. Biol. Chem 271 (1996) 25041-25048. [Medline UI: 96394681]


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