Continued from EC 2.7.2 and EC 2.7.3
EC 2.7.4 Phosphotransferases with a phosphate group as acceptor
EC 2.7.5 Phosphotransferases with regeneration of donors, apparently catalysing intramolecular transfers
EC 2.7.6 Diphosphotransferases
Accepted name: ATP-polyphosphate phosphotransferase
Reaction: ATP + (phosphate)n = ADP + (phosphate)n+1
Other name(s): polyphosphate kinase 1; ppk1 (gene name); polyphosphate kinase (ambiguous); polyphosphoric acid kinase (ambiguous)
Systematic name: ATP:polyphosphate phosphotransferase
Comments: The enzyme is responsible for the synthesis of most of the cellular polyphosphate, using the terminal phosphate of ATP as substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-44-2
References:
1. Hoffmann-Ostenhof, O., Kenedy, J., Keck, K., Gabriel, O. and Schönfellinger, H.W. En neues Phosphat-übertragendes Ferment aus Hefe. Biochim. Biophys. Acta 14 (1954) 285. [PMID: 13172250]
2. Kornberg, A., Kornberg, S.R. and Simms, E.S. Metaphosphate synthesis by an enzyme from Escherichia coli. Biochim. Biophys. Acta 20 (1956) 215-227. [PMID: 13315368]
3. Muhammed, A. Studies on biosynthesis of polymetaphosphate by an enzyme from Corynebacterium xerosis. Biochim. Biophys. Acta 54 (1961) 121-132. [PMID: 14476999]
4. Ahn, K. and Kornberg, A. Polyphosphate kinase from Escherichia coli. Purification and demonstration of a phosphoenzyme intermediate. J. Biol. Chem. 265 (1990) 11734-11739. [PMID: 2164013]
5. Kumble, K.D., Ahn, K. and Kornberg, A. Phosphohistidyl active sites in polyphosphate kinase of Escherichia coli. Proc. Natl. Acad. Sci. USA 93 (1996) 14391-14395. [PMID: 8962061]
Accepted name: phosphomevalonate kinase
Reaction: ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
For reaction pathway click here.
Other names: ATP:5-phosphomevalonate phosphotransferase; 5-phosphomevalonate kinase; mevalonate phosphate kinase; mevalonate-5-phosphate kinase; mevalonic acid phosphate kinase
Systematic name: ATP:(R)-5-phosphomevalonate phosphotransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-46-4
References:
1. Bloch, K., Chaykin, S., Phillips, A.H. and de Waard, A. Mevalonic acid pyrophosphate and isopentenyl pyrophosphate. J. Biol. Chem. 234 (1959) 2595-2604.
2. Henning, U., Möslein, E.M. and Lynen, F. Biosynthesis of terpenes. V. Formation of 5-pyrophosphomevalonic acid by phosphomevalonic kinase. Arch. Biochem. Biophys. 83 (1959) 259-267.
3. Levy, G.B. and Popják, G. Studies on the biosynthesis of cholesterol. 10. Mevalonic kinase and phosphomevalonic kinase from liver. Biochem. J. 75 (1960) 417-428.
Accepted name: adenylate kinase
Reaction: ATP + AMP = 2 ADP
Other name(s): myokinase; 5'-AMP-kinase; adenylic kinase; adenylokinase
Systematic name: ATP:AMP phosphotransferase
Comments: Inorganic triphosphate can also act as donor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9013-02-9
References:
1. Chiga, M. and Plaut, G.W.E. Nucleotide transphosphorylases from liver. I. Purification and properties of an adenosine triphosphate-adenosine monophosphate transphosphorylase from swine liver. J. Biol. Chem. 235 (1960) 3260-3265.
2. Saint Girons, I.S., Gilles, A.-M., Margarita, D., Michelson, S., Monnot, M., Fermandjian, S., Danchin, A. and Barzu, O. Structural and catalytic characteristics of Escherichia coli adenylate kinase. J. Biol. Chem. 262 (1987) 622-629. [PMID: 3027060]
3. Noda, L. Adenosine triphosphate-adenosine monophosphate transphosphorylase. III. Kinetic studies. J. Biol. Chem. 232 (1958) 237-250.
4. Noda, L. Nucleoside triphosphate-nucleoside monophosphokinases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp.139-149.
5. Noda, L. and Kuby, S.A. Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). I. Isolation of the crystalline enzyme from rabbit skeletal muscle. J. Biol. Chem. 226 (1957) 541-549.
6. Noda, L. and Kuby, S.A. Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). II. Homogeneity measurements and physicochemical properties. J. Biol. Chem. 226 (1957) 551-558.
7. Oliver, I.T. and Peel, J.L. Myokinase activity in microorganisms. Biochim. Biophys. Acta 20 (1956) 390-392.
Accepted name: nucleoside-phosphate kinase
Reaction: ATP + nucleoside phosphate = ADP + nucleoside diphosphate
For diagram of reaction click here.
Other names: NMP-kinase
Systematic name: ATP:nucleoside-phosphate phosphotransferase
Comments: Many nucleotides can act as acceptors; other nucleoside triphosphates can act instead of ATP.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-50-0
References:
1. Gibson, D.M., Ayengar, P. and Sanadi, D.R. Transphosphorylations between nucleoside phosphates. Biochim. Biophys. Acta 21 (1956) 86-91.
2. Heppel, L.A., Strominger, J.L. and Maxwell, E.S. Nucleoside monophosphate kinases. II. Transphosphorylation between adenosine monophosphate and nucleotide triphosphate. Biochim. Biophys. Acta 32 (1959) 422-430.
3.Lieberman, I., Kornberg, A. and Simms, E.S. Enzymatic synthesis of nucleotide diphosphates and triphosphates. J. Biol. Chem. 215 (1955) 429-440.
4. Noda, L. Nucleoside triphosphate-nucleoside monophosphokinases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp.139-149.
[EC 2.7.4.5 Deleted entry: deoxycytidylate kinase. Now included with EC 2.7.4.14 cytidylate kinase (EC 2.7.4.5 created 1961, deleted 1972)]
Accepted name: nucleoside-diphosphate kinase
Reaction: ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
For diagram of reaction click here.
Other names: nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase
Systematic name: ATP:nucleoside-diphosphate phosphotransferase
Comments: Many nucleoside diphosphates can act as acceptors, while many ribo- and deoxyribonucleoside triphosphates can act as donors.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-51-1
References:
1. Berg, P. and Joklik, W.K. Enzymatic phosphorylation of nucleoside diphosphates. J. Biol. Chem. 210 (1954) 657-672.
2. Gibson, D.M., Ayengar, P. and Sanadi, D.R. Transphosphorylations between nucleoside phosphates. Biochim. Biophys. Acta 21 (1956) 86-91.
3. Kirkland, R.J.A. and Turner, J.F. Nucleoside diphosphokinase of pea seeds. Biochem. J. 72 (1959) 716-720.
4. Krebs, H.A. and Hems, R. Some reactions of adenosine and inosine phosphates in animal tissues. Biochim. Biophys. Acta 12 (1953) 172-180.
5. Nakamura, H. and Sugino, Y. Metabolism of deoxyribonucleotides. 3. Purification and some properties of nucleoside diphosphokinase of calf thymus. J. Biol. Chem. 241 (1966) 4917-4922. [PMID: 5925862]
6. Ratliff, R.L., Weaver, R.H., Lardy, H.A. and Kuby, S.A. Nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). I. Isolation of the crystalline enzyme from brewers' yeast. J. Biol. Chem. 239 (1964) 301-309.
Accepted name: phosphooxymethylpyrimidine kinase
Reaction: ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine = ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
For diagram of reaction click here.
Other name(s): hydroxymethylpyrimidine phosphokinase; ATP:4-amino-2-methyl-5-phosphooxymethylpyrimidine phosphotransferase; ATP:(4-amino-2-methylpyrimidin-5-yl)methyl-phosphate phosphotransferase; phosphomethylpyrimidine kinase
Systematic name: ATP:4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-18-5
References:
1. Lewin, L.M. and Brown, G.M. The biosynthesis of thiamine. III. Mechanism of enzymatic formation of the pyrophosphate ester of 2-methyl-4-amino-5-hydroxymethylpyrimidine. J. Biol. Chem. 236 (1961) 2768-2771.
Accepted name: guanylate kinase
Reaction: ATP + GMP = ADP + GDP
For diagram of reaction click here.
Other name(s): deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase
Systematic name: ATP:(d)GMP phosphotransferase
Comments: dGMP can also act as acceptor, and dATP can act as donor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-59-9
References:
1. Buccino, R.J., Jr. and Roth, J.S. Partial purification and properties of ATP:GMP phosphotransferase from rat liver. Arch. Biochem. Biophys. 132 (1969) 49-61. [PMID: 4307347]
2. Hiraga, S. and Sugino, Y. Nucleoside monophosphokinases of Escherichia coli infected and uninfected with an RNA phage. Biochim. Biophys. Acta 114 (1966) 416-418.
3. Griffith, T.J. and Helleiner, C.W. The partial purification of deoxynucleoside monophosphate kinases from L cells. Biochim. Biophys. Acta 108 (1965) 114-124. [PMID: 5862227]
4. Oeschger, M.P. and Bessman, M.J. Purification and properties of guanylate kinase from Escherichia coli. J. Biol. Chem. 241 (1966) 5452-5460. [PMID: 5333666]
5. Shimono, H. and Sugino, Y. Metabolism of deoxyribonucleotides. Purification and properties of deoxyguanosine monophosphokinase of calf thymus. Eur. J. Biochem. 19 (1971) 256-263. [PMID: 5552394]
Accepted name: dTMP kinase
Reaction: ATP + dTMP = ADP + dTDP
Other names: thymidine monophosphate kinase; thymidylate kinase; thymidylate monophosphate kinase; thymidylic acid kinase; thymidylic kinase; deoxythymidine 5'-monophosphate kinase; TMPK; thymidine 5'-monophosphate kinase
Systematic name: ATP:dTMP phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-43-1
References:
1. Hurwitz, J. The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material. J. Biol. Chem. 234 (1959) 2351-2358.
2. Keilley, R.K. Purification and properties of thymidine monophosphate kinase from mouse hepatoma. J. Biol. Chem. 245 (1970) 4204-4212. [PMID: 4323166]
3. Nelson, D.J. and Carter, C.E. Purification and characterization of thymidine 5-monophosphate kinase from Escherichia coli B. J. Biol. Chem. 244 (1969) 5254-5262. [PMID: 4899016]
Accepted name: nucleoside-triphosphate—adenylate kinase
Reaction: nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
Other names: guanosine triphosphate-adenylate kinase; nucleoside triphosphate-adenosine monophosphate transphosphorylase; GTP:AMP phosphotransferase; isozyme 3 of adenylate kinase
Systematic name: nucleoside-triphosphate:AMP phosphotransferase
Comments: Many nucleoside triphosphates can act as donors.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-74-8
References:
1. Albrecht, G.J. Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria. Biochemistry 9 (1970) 2462-2770. [PMID: 5423264]
2. Chiga, M., Rogers, A.E. and Plaut, G.W.E. Nucleotide transphosphorylases from liver. II. Purification and properties of a 6-oxypurine nucleoside triphosphate-adenosine monophosphate transphosphorylase from swine liver. J. Biol. Chem. 236 (1961) 1800-1805.
Accepted name: (deoxy)adenylate kinase
Reaction: ATP + dAMP = ADP + dADP
Systematic name: ATP:(d)AMP phosphotransferase
Comments: AMP can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-19-6
References:
1. Griffith, T.J. and Helleiner, C.W. The partial purification of deoxynucleoside monophosphate kinases from L cells. Biochim. Biophys. Acta 108 (1965) 114-124. [PMID: 5862227]
Accepted name: T2-induced deoxynucleotide kinase
Reaction: ATP + dGMP (or dTMP) = ADP + dGDP (or dTDP)
Systematic name: ATP:(d)NMP phosphotransferase
Comments: dTMP and dAMP can act as acceptors; dATP can act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-99-2
References:
1. Bello, L.J. and Bessman, M.J. The enzymology of virus-infected bacteria. IV. Purification and properties of the deoxynucleotide kinase induced by bacteriophage T2. J. Biol. Chem. 238 (1963) 1777-1787.
Accepted name: (deoxy)nucleoside-phosphate kinase
Reaction: ATP + a 2′-deoxyribonucleoside 5′-phosphate = ADP + a 2′-deoxyribonucleoside 5′-diphosphate
Other name(s): deoxynucleoside monophosphate kinase; deoxyribonucleoside monophosphokinase; deoxynucleoside-5′-monophosphate kinase; ATP:deoxynucleoside-phosphate phosphotransferase
Systematic name: ATP:2′-deoxyribonucleoside-5′-phosphate phosphotransferase
Comments: dATP can substitute for ATP.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37278-20-9
References:
1. Bessman, M.J., Herriott, S.T. and Orr, M.J.V.B. The enzymology of virus-infected bacteria. VI. Purification and properties of the deoxynucleotide kinase induced by bacteriophage T5. J. Biol. Chem. 240 (1965) 439-445.
Accepted name: UMP/CMP kinase
Reaction: (1) ATP + (d)CMP = ADP + (d)CDP
(2) ATP + UMP = ADP + UDP
Other name(s): cytidylate kinase; deoxycytidylate kinase; CTP:CMP phosphotransferase; dCMP kinase; deoxycytidine monophosphokinase; UMP-CMP kinase; ATP:UMP-CMP phosphotransferase; pyrimidine nucleoside monophosphate kinase; uridine monophosphate-cytidine monophosphate phosphotransferase
Systematic name: ATP:CMP(UMP) phosphotransferase
Comments: This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37278-21-0
References:
1. Hurwitz, J. The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material. J. Biol. Chem. 234 (1959) 2351-2358. [PMID: 14405566]
2. Ruffner, B.W., Jr. and Anderson, E.P. Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis. J. Biol. Chem. 244 (1969) 5994-6002. [PMID: 5350952]
3. Scheffzek, K., Kliche, W., Wiesmuller, L. and Reinstein, J. Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 Å: implications for water-mediated specificity. Biochemistry 35 (1996) 9716-9727. [PMID: 8703943]
4. Zhou, L., Lacroute, F. and Thornburg, R. Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase. Plant Physiol. 117 (1998) 245-254. [PMID: 9576794]
5. Van Rompay, A.R., Johansson, M. and Karlsson, A. Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme. Mol. Pharmacol. 56 (1999) 562-569. [PMID: 10462544]
Accepted name: thiamine-diphosphate kinase
Reaction: ATP + thiamine diphosphate = ADP + thiamine triphosphate
For diagram of reaction click here.
Glossary: thiamine diphosphate
Other names: ATP:thiamin-diphosphate phosphotransferase; TDP kinase; thiamin diphosphate kinase; thiamin diphosphate phosphotransferase; thiamin pyrophosphate kinase; thiamine diphosphate kinase; protein bound thiamin diphosphate:ATP phosphoryltransferase
Systematic name: ATP:thiamine-diphosphate phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-79-0
References:
1. Itokawa, Y. and Cooper, J.R. The enzymatic synthesis of triphosphothiamin. Biochim. Biophys. Acta 158 (1968) 180-182. [PMID: 5661031]
2. Kikuchi, M. and Ikawa, T. Presence of an enzyme mediating transfer of phosphate from thiamine triphosphate to ADP in germinating maize. Bot. Mag. (Tokyo) 97 (1984) 193-205.
Accepted name: thiamine-phosphate kinase
Reaction: ATP + thiamine phosphate = ADP + thiamine diphosphate
For diagram of reaction click here.
Glossary: thiamine diphosphate
Other name(s): thiamin-monophosphate kinase; thiamin monophosphatase; thiamin monophosphokinase
Systematic name: ATP:thiamine-phosphate phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-23-9
References:
1. Nishino, H. Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase. J. Biochem. (Tokyo) 72 (1972) 1093-1100. [PMID: 4567662]
Accepted name: 3-phosphoglyceroyl-phosphate—polyphosphate phosphotransferase
Reaction: 3-phospho-D-glyceroyl phosphate + (phosphate)n = 3-phosphoglycerate + (phosphate)n+1
Other names: diphosphoglycerate-polyphosphate phosphotransferase; 1,3-diphosphoglycerate-polyphosphate phosphotransferase
Systematic name: 3-phospho-D-glyceroyl-phosphate:polyphosphate phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9055-36-1
References:
1. Kulaev, I.S. and Bobyk, M.A. Detection of a new enzyme in Neurospora crassa - 1,3-diphosphoglycerate:polyphosphatephosphotransferase. Biochemistry (Moscow) 36 (1971) 356-359.
2. Kulaev, I.S., Bobyk, M.A., Nikolaev, N.N., Sergeev, N.S. and Uryson, S.O. Polyphosphate synthesizing enzymes in some fungi and bacteria. Biochemistry (Moscow) 36 (1971) 791-796.
Accepted name: farnesyl-diphosphate kinase
Reaction: ATP + farnesyl diphosphate = ADP + farnesyl triphosphate
Other names: farnesyl pyrophosphate kinase
Systematic name: ATP:farnesyl-diphosphate phosphotransferase
Comments: ADP can also act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 50936-43-1
References:
1. Schechter, I. Phosphate transfer from trans-farnesyl triphosphate to AMP in Gibberella fujikuroi. Biochim. Biophys. Acta 362 (1974) 233-244. [PMID: 4423368]
Accepted name: 5-methyldeoxycytidine-5'-phosphate kinase
Reaction: ATP + 5-methyldeoxycytidine 5'-phosphate = ADP + 5-methyldeoxycytidine diphosphate
Systematic name: ATP:5-methyldeoxycytidine-5'-phosphate phosphotransferase
Comments: The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts m5dCMP into m5dCDP and then into m5dCTP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81032-53-3
References:
1. Wang, R.Y.-H., Huang, L.-H. and Ehrlich, M. A bacteriophage-induced 5-methyldeoxycytidine 5'-monophosphate kinase. Biochim. Biophys. Acta 696 (1982) 31-36. [PMID: 7082669]
Accepted name: dolichyl-diphosphate—polyphosphate phosphotransferase
Reaction: dolichyl diphosphate + (phosphate)n = dolichyl phosphate + (phosphate)n+1
Other names: dolichylpyrophosphate:polyphosphate phosphotransferase
Systematic name: dolichyl-diphosphate:polyphosphate phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 94949-27-6
References:
1. Naumov, A.V., Shabalin, Y.A., Vagabov, V.M. and Kulaev, I.S. Two pathways of dephosphorylation of dolichyl diphosphate in yeasts. Biochemistry (Moscow) 50 (1985) 551-556.
Accepted name: inositol-hexakisphosphate 5-kinase
Reaction: (1) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
(2) ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
Other name(s): ATP:1D-myo-inositol-hexakisphosphate phosphotransferase; IP6K; inositol-hexakisphosphate kinase (ambiguous)
Systematic name: ATP:1D-myo-inositol-hexakisphosphate 5-phosphotransferase
Comments: Three mammalian isoforms are known to exist.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 176898-37-6
References:
1. Saiardi, A., Erdjument-Bromage, H., Snowman, A.M., Tempst, P. and Snyder, S.H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9 (1999) 1323-1326. [PMID: 10574768]
2. Schell, M.J., Letcher, A.J., Brearley, C.A., Biber, J., Murer, H. and Irvine, R.F. PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase. FEBS Lett. 461 (1999) 169-172. [PMID: 10567691]
3. Albert, C., Safrany, S.T., Bembenek, M.E., Reddy, K.M., Reddy, K.K., Falck, J.-R., Bröcker, M., Shears, S.B. and Mayr, G.W. Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (1997) 553-560. [PMID: 9359429]
4. Lin, H., Fridy, P.C., Ribeiro, A.A., Choi, J.H., Barma, D.K., Vogel, G., Falck, J.R., Shears, S.B., York, J.D. and Mayr, G.W. Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases. J. Biol. Chem. 284 (2009) 1863-1872. [PMID: 18981179]
5. Wang, H., Falck, J.R., Hall, T.M. and Shears, S.B. Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nat. Chem. Biol. 8 (2012) 111-116. [PMID: 22119861]
Accepted name: UMP kinase
Reaction: ATP + UMP = ADP + UDP
Other name(s): uridylate kinase; UMPK; uridine monophosphate kinase; PyrH; UMP-kinase; SmbA
Systematic name: ATP:UMP phosphotransferase
Comments: This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9036-23-1
References:
1. Serina, L., Blondin, C., Krin, E., Sismeiro, O., Danchin, A., Sakamoto, H., Gilles, A.M. and B̢rzu O. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP. Biochemistry 34 (1995) 5066-5074. [PMID: 7711027]
2. Marco-Marin, C., Gil-Ortiz, F. and Rubio, V. The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis. J. Mol. Biol. 352 (2005) 438-454. [PMID: 16095620]
Accepted name: ribose 1,5-bisphosphate phosphokinase
Reaction: ATP + α-D-ribose 1,5-bisphosphate = ADP + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction click here.
Glossary: PRPP = 5-phospho-α-D-ribose 1-diphosphate
Other name(s): ribose 1,5-bisphosphokinase; PhnN; ATP:ribose-1,5-bisphosphate phosphotransferase
Systematic name: ATP:α-D-ribose-1,5-bisphosphate phosphotransferase
Comments: This enzyme, found in NAD supression mutants of Escherichia coli, synthesizes 5-phospho-α-D-ribose 1-diphosphate (PRPP) without the participation of EC 2.7.6.1, ribose-phosphate diphosphokinase. Ribose, ribose 1-phosphate and ribose 5-phosphate are not substrates, and GTP cannot act as a phosphate donor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hove-Jensen, B., Rosenkrantz, T.J., Haldimann, A. and Wanner, B.L. Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways. J. Bacteriol. 185 (2003) 2793-2801. [PMID: 12700258]
Accepted name: diphosphoinositol-pentakisphosphate 1-kinase
Reaction: (1) ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
(2) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
Other name(s): PP-IP5 kinase; diphosphoinositol pentakisphosphate kinase; ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase; PP-InsP5 kinase; PPIP5K; PPIP5K1; PPIP5K2; VIP1; VIP2; diphosphoinositol-pentakisphosphate 1/3-kinase (incorrect); diphosphoinositol-pentakisphosphate kinase (ambiguous)
Systematic name: ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate 1-phosphotransferase
Comments: This enzyme is activated by osmotic shock [4]. Ins(1,3,4,5,6)P5, 1D-myo-inositol diphosphate tetrakisphosphate and 1D-myo-inositol bisdiphosphate triphosphate are not substrates [4]. The enzyme specifically phosphorylates the 1-position of the substrates [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Shears, S.B., Ali, N., Craxton, A. and Bembenek, M.E. Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo. J. Biol. Chem. 270 (1995) 10489-10497. [PMID: 7737983]
2. Albert, C., Safrany, S.T., Bembenek, M.E., Reddy, K.M., Reddy, K.K., Falck, J.-R., Bröcker, M., Shears, S.B. and Mayr, G.W. Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (1997) 553-560. [PMID: 9359429]
3. Fridy, P.C., Otto, J.C., Dollins, D.E. and York, J.D. Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases. J. Biol. Chem. 282 (2007) 30754-30762. [PMID: 17690096]
4. Choi, J.H., Williams, J., Cho, J., Falck, J.R. and Shears, S.B. Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that Is activated when cells are exposed to hyperosmotic stress. J. Biol. Chem. 282 (2007) 30763-30775. [PMID: 17702752]
5. Lin, H., Fridy, P.C., Ribeiro, A.A., Choi, J.H., Barma, D.K., Vogel, G., Falck, J.R., Shears, S.B., York, J.D. and Mayr, G.W. Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases. J. Biol. Chem. 284 (2009) 1863-1872. [PMID: 18981179]
6. Wang, H., Falck, J.R., Hall, T.M. and Shears, S.B. Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nat. Chem. Biol. 8 (2012) 111-116. [PMID: 22119861]
Accepted name: (d)CMP kinase
Reaction: ATP + (d)CMP = ADP + (d)CDP
Glossary: CMP = cytidine monophosphate
dCMP = deoxycytidine monophosphate
CDP = cytidine diphosphate
dCDP = deoxycytidine diphosphate
UMP = uridine monophosphate
UDP = uridine diphosphate
Other name(s): prokaryotic cytidylate kinase; deoxycytidylate kinase; dCMP kinase; deoxycytidine monophosphokinase
Systematic name: ATP:(d)CMP phosphotransferase
Comments: The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Bertrand, T., Briozzo, P., Assairi, L., Ofiteru, A., Bucurenci, N., Munier-Lehmann, H., Golinelli-Pimpaneau, B., Barzu, O. and Gilles, A.M. Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. J. Mol. Biol. 315 (2002) 1099-1110. [PMID: 11827479]
2. Thum, C., Schneider, C.Z., Palma, M.S., Santos, D.S. and Basso, L.A. The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP. J. Bacteriol. 191 (2009) 2884-2887. [PMID: 19181797]
Accepted name: isopentenyl phosphate kinase
Reaction: ATP + 3-methylbut-3-en-1-yl phosphate = ADP + 3-methylbut-3-en-1-yl diphosphate
For diagram of reaction click here.
Systematic name: ATP:3-methylbut-3-en-1-yl-phosphate phosphotransferase
Comments: The enzyme is involved in the mevalonate pathway in Archaea [1]. The activity has also been identified in the plant Mentha piperita (peppermint) [2]. It is strictly specific for ATP but can use other phosphate acceptors such as dimethylallyl phosphate, geranyl phosphate, or fosfomycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Grochowski, L.L., Xu, H. and White, R.H. Methanocaldococcus jannaschii uses a modified mevalonate pathway for biosynthesis of isopentenyl diphosphate. J. Bacteriol. 188 (2006) 3192-3198. [PMID: 16621811]
2. Lange, B.M. and Croteau, R. Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step. Proc. Natl. Acad. Sci. USA 96 (1999) 13714-13719. [PMID: 10570138]
3. Chen, M. and Poulter, C.D. Characterization of thermophilic archaeal isopentenyl phosphate kinases. Biochemistry 49 (2010) 207-217. [PMID: 19928876]
4. Mabanglo, M.F., Schubert, H.L., Chen, M., Hill, C.P. and Poulter, C.D. X-ray structures of isopentenyl phosphate kinase. ACS Chem. Biol. 5 (2010) 517-527. [PMID: 20402538]
Accepted name: [pyruvate, phosphate dikinase]-phosphate phosphotransferase
Reaction: [pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate
Other name(s): PPDK regulatory protein (ambiguous); pyruvate, phosphate dikinase regulatory protein (ambiguous); bifunctional dikinase regulatory protein (ambiguous); PDRP1 (gene name)
Systematic name: [pyruvate, phosphate dikinase]-phosphate:phosphate phosphotransferase
Comments: The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyses the phosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.11.32, [pyruvate, phosphate dikinase] kinase [2-5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Burnell, J.N. and Hatch, M.D. Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase. Arch. Biochem. Biophys. 231 (1984) 175-182. [PMID: 6326674]
2. Burnell, J.N. and Hatch, M.D. Regulation of C4 photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase. Arch. Biochem. Biophys. 237 (1985) 490-503. [PMID: 2983615]
3. Chastain, C.J., Botschner, M., Harrington, G.E., Thompson, B.J., Mills, S.E., Sarath, G. and Chollet, R. Further analysis of maize C4 pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues. Arch. Biochem. Biophys. 375 (2000) 165-170. [PMID: 10683263]
4. Burnell, J.N. and Chastain, C.J. Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene. Biochem. Biophys. Res. Commun. 345 (2006) 675-680. [PMID: 16696949]
5. Chastain, C.J., Xu, W., Parsley, K., Sarath, G., Hibberd, J.M. and Chollet, R. The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure. Plant J. 53 (2008) 854-863. [PMID: 17996018]
Accepted name: [pyruvate, water dikinase]-phosphate phosphotransferase
Reaction: [pyruvate, water dikinase] phosphate + phosphate = [pyruvate, water dikinase] + diphosphate
Other name(s): PSRP (ambiguous)
Systematic name: [pyruvate, water dikinase]-phosphate:phosphate phosphotransferase
Comments: The enzyme from the bacterium Escherichia coli is bifunctional and catalyses both the phosphorylation and dephosphorylation of EC 2.7.9.2, pyruvate, water dikinase. cf. EC 2.7.11.33, [pyruvate, water dikinase] kinase [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Burnell, J.N. Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria. BMC Biochem. 11 (2010) 1. [PMID: 20044937]
Accepted name: Kdo2-lipid A phosphotransferase
Reaction: ditrans-octacis-undecaprenyl diphosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A = ditrans-octacis-undecaprenyl phosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A 1-diphosphate
Glossary: lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A 1-diphosphate =
2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl diphosphate
Other name(s): lipid A undecaprenyl phosphotransferase; LpxT; YeiU
Systematic name: ditrans-octacis-undecaprenyl-diphosphate:α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid-A phosphotransferase
Comments: An inner-membrane protein. The activity of the enzyme is regulated by PmrA. In vitro the enzyme can use diacylglycerol 3-diphosphate as the phosphate donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Touze, T., Tran, A.X., Hankins, J.V., Mengin-Lecreulx, D. and Trent, M.S. Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate. Mol. Microbiol. 67 (2008) 264-277. [PMID: 18047581]
2. Herrera, C.M., Hankins, J.V. and Trent, M.S. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol. Microbiol. 76 (2010) 1444-1460. [PMID: 20384697]
[EC 2.7.4.30 Transferred entry: lipid A phosphoethanolamine transferase, now EC 2.7.8.43, lipid A phosphoethanolamine transferase (EC 2.7.4.30 created 2015, deleted 2016)]
Accepted name: [5-(aminomethyl)furan-3-yl]methyl phosphate kinase
Reaction: ATP + [5-(aminomethyl)furan-3-yl]methyl phosphate = ADP + [5-(aminomethyl)furan-3-yl]methyl diphosphate
For diagram of reaction click here.
Other name(s): MfnE
Systematic name: ATP:[5-(aminomethyl)furan-3-yl]methyl-phosphate phosphotransferase
Comments: Requires Mg2+. The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wang, Y., Xu, H., Jones, M.K. and White, R.H. Identification of the final two genes functioning in methanofuran biosynthesis in Methanocaldococcus jannaschii. J. Bacteriol. 197 (2015) 2850-2858. [PMID: 26100040]
Accepted name: farnesyl phosphate kinase
Reaction: CTP + (2E,6E)-farnesyl phosphate = CDP + (2E,6E)-farnesyl diphosphate
For diagram of reaction click here.
Systematic name: CTP:(2E,6E)-farnesyl-phosphate phosphotransferase
Comments: The enzyme, found in plants and animals, is specific for CTP as phosphate donor. It does not use farnesol as substrate (cf. EC 2.7.1.216, farnesol kinase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bentinger, M., Grunler, J., Peterson, E., Swiezewska, E. and Dallner, G. Phosphorylation of farnesol in rat liver microsomes: properties of farnesol kinase and farnesyl phosphate kinase. Arch. Biochem. Biophys. 353 (1998) 191-198. [PMID: 9606952]
2. Fitzpatrick, A.H., Bhandari, J. and Crowell, D.N. Farnesol kinase is involved in farnesol metabolism, ABA signaling and flower development in Arabidopsis. Plant J. 66 (2011) 1078-1088. [PMID: 21395888]
Accepted name: AMP-polyphosphate phosphotransferase
Reaction: ADP + (phosphate)n = AMP + (phosphate)n+1
Other name(s): PA3455 (locus name); PPK2D; PAP
Systematic name: ADP:polyphosphate phosphotransferase
Comments: The enzyme, characterized from the bacteria Acinetobacter johnsonii and Pseudomonas aeruginosa, transfers a phosphate group from polyphosphates to nucleotide monophosphates. The highest activity is achieved with AMP, but the enzyme can also phosphorylate GMP, dAMP, dGMP, IMP, and XMP. The reverse reactions were not detected.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bonting, C.F., Kortstee, G.J. and Zehnder, A.J. Properties of polyphosphate: AMP phosphotransferase of Acinetobacter strain 210A. J. Bacteriol. 173 (1991) 6484-6488. [PMID: 1655714]
2. Shiba, T., Itoh, H., Kameda, A., Kobayashi, K., Kawazoe, Y. and Noguchi, T. Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent nucleoside monophosphate kinase in Acinetobacter johnsonii 210A. J. Bacteriol. 187 (2005) 1859-1865. [PMID: 15716459]
3. Nocek, B., Kochinyan, S., Proudfoot, M., Brown, G., Evdokimova, E., Osipiuk, J., Edwards, A.M., Savchenko, A., Joachimiak, A. and Yakunin, A.F. Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. Proc. Natl. Acad. Sci. USA 105 (2008) 17730-17735. [PMID: 19001261]
Accepted name: GDP-polyphosphate phosphotransferase
Reaction: GTP + (phosphate)n = GDP + (phosphate)n+1
Other name(s): ppk2 (gene name); polyphosphate kinase 2
Systematic name: GTP:polyphosphate phosphotransferase
Comments: Polyphosphate kinase 2, characterized from the bacterium Pseudomonas aeruginosa, uses inorganic polyphosphate as a donor to convert GDP to GTP. The enzyme can also act on ADP (cf. EC 2.7.4.1, ATP-polyphosphate phosphotransferase), but with lower activity. The enzyme has only a trivial activity in the opposite direction (synthesizing polyphosphate from GTP). The GTP that is produced is believed to be consumed by EC 2.7.7.13, mannose-1-phosphate guanylyltransferase, for production of alginate during stationary phase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, H., Ishige, K. and Kornberg, A. A polyphosphate kinase (PPK2) widely conserved in bacteria. Proc. Natl. Acad. Sci. USA 99 (2002) 16678-16683. [PMID: 12486232]
2. Ishige, K., Zhang, H. and Kornberg, A. Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP. Proc. Natl. Acad. Sci. USA 99 (2002) 16684-16688. [PMID: 12482933]
EC 2.7.5 In the early editions of Enzyme Nomenclature, phosphomutases were listed here under the heading 'Phosphotransferases with regeneration of donors, apparently catalysing intramolecular transfers'. They are now listed in sub-subgroup 5.4.2 on the basis of the overall isomerization reaction.
[EC 2.7.5.1 Transferred entry: now EC 5.4.2.2 phosphoglucomutase (EC 2.7.5.1 created 1961, deleted 1984)]
[EC 2.7.5.2 Transferred entry: now EC 5.4.2.3 phosphoacetylglucosamine mutase (EC 2.7.5.2 created 1961, deleted 1984)]
[EC 2.7.5.3 Transferred entry: now EC 5.4.2.1 phosphoglyceromutase (EC 2.7.5.3 created 1961, deleted 1984)]
[EC 2.7.5.4 Transferred entry: now EC 5.4.2.4 bisphosphoglyceromutase (EC 2.7.5.4 created 1961, deleted 1984)]
[EC 2.7.5.5 Transferred entry: now EC 5.4.2.5 phosphoglucomutase (glucose-cofactor) (EC 2.7.5.5 created 1972, deleted 1984)]
[EC 2.7.5.6 Transferred entry: now EC 5.4.2.7 phosphopentomutase (EC 2.7.5.6 created 1972, deleted 1984)]
[EC 2.7.5.7 Transferred entry: now EC 5.4.2.8 phosphomannomutase (EC 2.7.5.7 created 1981, deleted 1984)]
Accepted name: ribose-phosphate diphosphokinase
Reaction: ATP + D-ribose 5-phosphate = AMP + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction click here.
Glossary: PRPP = 5-phospho-α-D-ribose 1-diphosphate
Other name(s): ribose-phosphate pyrophosphokinase; PRPP synthetase; phosphoribosylpyrophosphate synthetase; PPRibP synthetase; PP-ribose P synthetase; 5-phosphoribosyl-1-pyrophosphate synthetase; 5-phosphoribose pyrophosphorylase; 5-phosphoribosyl-alpha-1-pyrophosphate synthetase; phosphoribosyl-diphosphate synthetase; phosphoribosylpyrophosphate synthase; pyrophosphoribosylphosphate synthetase; ribophosphate pyrophosphokinase; ribose-5-phosphate pyrophosphokinase
Systematic name: ATP:D-ribose-5-phosphate diphosphotransferase
Comments: dATP can also act as donor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9015-83-2
References:
1. Hughes, D.E. and Williamson, D.H. Some properties of glutaminase of Clostridium welchii. Biochem. J. 51 (1952) 45-55.
2. Hurlbert, R.B. and Reichard, P. The conversion of orotic acid to uridine nucleotides in vitro. Acta Chem. Scand. 9 (1955) 251-262.
3. Remy, C.N., Remy, W.T. and Buchanan, J.M. Biosynthesis of the purines. VIII. Enzymatic synthesis and utilization of α-5-phosphoribosylpyrophosphate. J. Biol. Chem. 217 (1955) 885-895.
4. Switzer, R.L. Regulation and mechanism of phosphoribosylpyrophosphate synthetase. I. Purification and properties of the enzyme from Salmonella typhimurium. J. Biol. Chem. 244 (1969) 2854-2863. [PMID: 4306285]
Accepted name: thiamine diphosphokinase
Reaction: ATP + thiamine = AMP + thiamine diphosphate
Glossary: thiamine diphosphate
Other name(s): thiamin kinase; thiamine pyrophosphokinase; ATP:thiamin pyrophosphotransferase; thiamin pyrophosphokinase; thiamin pyrophosphotransferase; thiaminokinase; thiamin:ATP pyrophosphotransferase; TPTase
Systematic name: ATP:thiamine diphosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-24-8
References:
1. Leuthardt, F. and Nielsen, H. Phosphorylation biologique de la thiamine. Helv. Chim. Acta 35 (1952) 1196-1209.
2. Shimazono, N., Mano, Y., Tanaka, R. and Kajiro, Y. Mechanism of transpyrophosphorylation with thiamine pyrophosphokinase. J. Biochem. (Tokyo) 46 (1959) 959-961.
3. Steyn-Parvé, E.P. Partial purification and properties of thiaminokinase from yeast. Biochim. Biophys. Acta 8 (1952) 310-324.
Accepted name: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
Reaction: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
For diagram of reaction click here or click here.
Other name(s): 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; H2-pteridine-CH2OH pyrophosphokinase; 7,8-dihydroxymethylpterin-pyrophosphokinase; HPPK; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hydroxymethyldihydropteridine pyrophosphokinase; ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase
Systematic name: ATP:6-hydroxymethyl-7,8-dihydropterin 6'-diphosphotransferase
Comments: Binds 2 Mg2+ ions that are essential for activity [4]. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants, fungi, and some archaeal species, including the haloarchaea) and methanopterin (in some archaeal species such as the Archaeoglobi and Methanobacteria). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase [4], the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase [7], while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-23-2
References:
1. Shiota, T., Baugh, C.M., Jackson, R. and Dillard, R. The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate. Biochemistry 8 (1969) 5022-5028. [PMID: 4312465]
2. Richey, D.P. and Brown, G.M. The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid. J. Biol. Chem. 244 (1969) 1582-1592. [PMID: 4304228]
3. Richey, D.P. and Brown, G.M. Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate synthetase from Escherichia coli. Methods Enzymol. 18B (1971) 765-771.
4. Lopez, P. and Lacks, S.A. A bifunctional protein in the folate biosynthetic pathway of Streptococcus pneumoniae with dihydroneopterin aldolase and hydroxymethyldihydropterin pyrophosphokinase activities. J. Bacteriol. 175 (1993) 2214-2220. [PMID: 8385663]
5. Blaszczyk, J., Shi, G., Yan, H. and Ji, X. Catalytic center assembly of HPPK as revealed by the crystal structure of a ternary complex at 1.25 Å resolution. Structure 8 (2000) 1049-1058. [PMID: 11080626]
6. Güldener, U., Koehler, G.J., Haussmann, C., Bacher, A., Kricke, J., Becher, D. and Hegemann, J.H. Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth. Mol. Biol. Cell 15 (2004) 3811-3828. [PMID: 15169867]
7. Storozhenko, S., Navarrete, O., Ravanel, S., De Brouwer, V., Chaerle, P., Zhang, G.F., Bastien, O., Lambert, W., Rebeille, F. and Van Der Straeten, D. Cytosolic hydroxymethyldihydropterin pyrophosphokinase/dihydropteroate synthase from Arabidopsis thaliana: a specific role in early development and stress response. J. Biol. Chem. 282 (2007) 10749-10761. [PMID: 17289662]
Accepted name: nucleotide diphosphokinase
Reaction: ATP + nucleoside 5'-phosphate = AMP + 5'-phosphonucleoside 3'-diphosphate
Other name(s): nucleotide pyrophosphokinase; ATP:nucleotide pyrophosphotransferase; ATP nucleotide 3'-pyrophosphokinase; nucleotide 3'-pyrophosphokinase
Systematic name: ATP:nucleoside-5'-phosphate diphosphotransferase
Comments: The enzyme acts on the 5'-mono-, di- and triphosphate derivatives of purine nucleosides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 53167-92-3
References:
1. Murao, S. and Nishino, T. Isolation and identification of ATP:nucleotide pyrophosphotransferase-producing microorganism. Agric. Biol. Chem. 38 (1974) 2483-2489.
2. Nishino, T. and Murao, S. Purification and some properties of ATP:nucleotide pyrophosphotransferase of Streptomyces adephospholyticus. Agric. Biol. Chem. 38 (1974) 2491-2496.
3. Nishino, T. and Murao, S. Characterization of pyrophosphoryl transfer reaction of ATP:nucleotide pyrophosphotransferase. Agric. Biol. Chem. 39 (1975) 1007-1014.
Accepted name: GTP diphosphokinase
Reaction: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
Other name(s): stringent factor; guanosine 3',5'-polyphosphate synthase; GTP pyrophosphokinase; ATP-GTP 3'-diphosphotransferase; guanosine 5',3'-polyphosphate synthetase; (p)ppGpp synthetase I; (p)ppGpp synthetase II; guanosine pentaphosphate synthetase; GPSI; GPSII
Systematic name: ATP:GTP 3'-diphosphotransferase
Comments: GDP can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 63690-89-1
References:
1. Fehr, S. and Richter, D. Stringent response of Bacillus stearothermophilus: evidence for the existence of two distinct guanosine 3',5'-polyphosphate synthetases. J. Bacteriol. 145 (1981) 68-73. [PMID: 6161916]
2. Sy, J. and Akers, H. Purification and properties of guanosine 5',3'-polyphosphate synthetase from Bacillus brevis. Biochemistry 15 (1976) 4399-4403. [PMID: 184817]