See separate file for EC 2.7.1.101 to EC 2.7.1.150,
EC 2.7.1.151 to EC 2.7.1.239.
Continued with:
EC 2.7.1.101 to EC 2.7.1.150
EC 2.7.1.151 to EC 2.7.1.239
Accepted name: L-fuculokinase
Reaction: ATP + L-fuculose = ADP + L-fuculose 1-phosphate
Other name(s): L-fuculokinase (phosphorylating); L-fuculose kinase
Systematic name: ATP:L-fuculose 1-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-64-6
References:
1. Heath, E.C. and Ghalambor, M.A. The metabolism of L-fucose. I. The purification and properties of L-fuculose kinase. J. Biol. Chem. 237 (1962) 2423-2426.
Accepted name: fucokinase
Reaction: ATP + L-fucose = ADP + β-L-fucose 1-phosphate
For diagram click here.
Other name(s): fucokinase (phosphorylating); fucose kinase; L-fucose kinase; L-fucokinase; ATP:6-deoxy-L-galactose 1-phosphotransferase; ATP:L-fucose 1-phosphotransferase
Systematic name: ATP:β-L-fucose 1-phosphotransferase
Comments: Requires a divalent cation for activity, with Mg2+ and Fe2+ giving rise to the highest enzyme activity. Forms part of a salvage pathway for reutilization of L-fucose. Can also phosphorylate D-arabinose, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-00-5
References:
1. Ishihara, H., Massaro, D.J. and Heath, E.C. The metabolism of L-fucose. 3. The enzymatic synthesis of β-L-fucose 1-phosphate. J. Biol. Chem. 243 (1968) 1103-1109. [PMID: 5646161]
2. Butler, W. and Serif, G.S. Fucokinase, its anomeric specificity and mechanism of phosphate group transfer. Biochim. Biophys. Acta 829 (1985) 238-243. [PMID: 2986701]
3. Park, S.H., Pastuszak, I., Drake, R. and Elbein, A.D. Purification to apparent homogeneity and properties of pig kidney L-fucose kinase. J. Biol. Chem. 273 (1998) 5685-5691. [PMID: 9488699]
Accepted name: L-xylulokinase
Reaction: ATP + L-xylulose = ADP + L-xylulose 5-phosphate
Other name(s): L-xylulokinase (phosphorylating)
Systematic name: ATP:L-xylulose 5-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-01-6
References:
1. Anderson, R.L. and Wood, W.A. Purification and properties of L-xylulokinase. J. Biol. Chem. 237 (1962) 1029-1033.
Accepted name: D-arabinokinase
Reaction: ATP + D-arabinose = ADP + D-arabinose 5-phosphate
For diagram of reaction click here.
Other name(s): D-arabinokinase (phosphorylating)
Systematic name: ATP:D-arabinose 5-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-02-7
References:
1. Volk, W.A. Purification and properties of D-arabinokinase from Propionibacterium pentosaceum. J. Biol. Chem. 237 (1962) 19-23.
Accepted name: allose kinase
Reaction: ATP + D-allose = ADP + D-allose 6-phosphate
Other name(s): allokinase (phosphorylating); allokinase; D-allokinase; D-allose-6-kinase
Systematic name: ATP:D-allose 6-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-78-1
References:
1. Gibbins, L.N. and Simpson, F.J. The purification and properties of D-allose-6-kinase from Aerobacter aerogenes. Can. J. Microbiol. 9 (1963) 769-779.
Accepted name: 1-phosphofructokinase
Reaction: ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate
Other name(s): fructose-1-phosphate kinase; 1-phosphofructokinase (phosphorylating); D-fructose-1-phosphate kinase; fructose 1-phosphate kinase; phosphofructokinase 1
Systematic name: ATP:D-fructose-phosphate 6-phosphotransferase
Comments: ITP, GTP or UTP can replace ATP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-03-8
References:
1. Reeves, R.E., Warren, L.G. and Hsu, D.S. 1-Phosphofructokinase from an anaerobe. J. Biol. Chem. 241 (1966) 1257-1261. [PMID: 4222878]
2. Sapico, V. and Anderson, R.L. D-Fructose 1-phosphate kinase and D-fructose 6-phosphate kinase from Aerobacter aerogenes. A comparative study of regulatory properties. J. Biol. Chem. 244 (1969) 6280-6288. [PMID: 4242639]
[EC 2.7.1.57 Deleted entry: mannitol kinase (EC 2.7.1.57 created 1972, deleted 1984)]
Accepted name: 2-dehydro-3-deoxygalactonokinase
Reaction: ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
For diagram of reaction click here.
Other name(s): 2-keto-3-deoxygalactonokinase; 2-keto-3-deoxygalactonate kinase (phosphorylating); 2-oxo-3-deoxygalactonate kinase;
Systematic name: ATP:2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-05-0
References:
1. Stouthamer, A.H. Glucose and galactose metabolism in Gluconobacter liquefaciens. Biochim. Biophys. Acta 48 (1961) 484-500.
Accepted name: N-acetylglucosamine kinase
Reaction: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate
Other name(s): acetylglucosamine kinase (phosphorylating); ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase; 2-acetylamino-2-deoxy-D-glucose kinase; acetylaminodeoxyglucokinase
Systematic name: ATP:N-acetyl-D-glucosamine 6-phosphotransferase
Comments: The bacterial enzyme also acts on D-glucose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-48-9
References:
1. Asensio, C. and Ruiz-Amil, M. N-Acetyl-D-glucosamine kinase. II. Escherichia coli. Methods Enzymol. 9 (1966) 421-425.
2. Barkulis, S.S. N-Acetyl-D-glucosamine kinase. I. Streptococcus pyrogenes. Methods Enzymol. 9 (1966) 415-420.
3. Datta, A. Studies on hog spleen N-acetylglucosamine kinase. I. Purification and properties of N-acetylglucosamine kinase. Biochim. Biophys. Acta 220 (1970) 51-60. [PMID: 4319609]
Accepted name: N-acylmannosamine kinase
Reaction: ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate
For diagram of reaction click here.
Other name(s): acylmannosamine kinase (phosphorylating); acetylamidodeoxymannokinase; acetylmannosamine kinase; acylaminodeoxymannokinase; acylmannosamine kinase; N-acyl-D-mannosamine kinase; N-acetylmannosamine kinase; ATP:N-acetylmannosamine 6-phosphotransferase
Systematic name: ATP:N-acyl-D-mannosamine 6-phosphotransferase
Comments: Acts on the acetyl and glycolyl derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-53-6
References:
1. Banerjee, S. and Ghosh, S. Purification and properties of N-acetylmannosamine kinase from Salmonella typhimurium. Eur. J. Biochem. 8 (1969) 200-206. [PMID: 4889177]
2. Ghosh, S. and Roseman, S. Enzymatic phosphorylation of N-acetyl-D-mannosamine. Proc. Natl. Acad. Sci. USA 47 (1961) 955-958.
3. Kundig, W., Ghosh, S. and Roseman, S. The sialic acids. VII. N-Acyl-D-mannosamine kinase from rat liver. J. Biol. Chem. 241 (1966) 5619-5626. [PMID: 5928201]
Accepted name: acyl-phosphate—hexose phosphotransferase
Reaction: acyl phosphate + D-hexose = a carboxylate + D-hexose phosphate
Other name(s): hexose phosphate:hexose phosphotransferase
Systematic name: acyl-phosphate:D-hexose phosphotransferase
Comments: Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1 or O-6.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-06-1
References:
1. Anderson, R.L. and Kamel, M.Y. Acyl phosphate:hexose phosphotransferase (hexose phosphate:hexose phosphotransferase). Methods Enzymol. 9 (1966) 392-396.
2. Kamel, M.Y. and Anderson, R.L. Acyl phosphate: hexose phosphotransferase. Purification and properties of the enzyme from Aerobacter aerogenes and evidence for its common identity with hexose phosphate: hexose phosphotransferase. Arch. Biochem. Biophys. 120 (1967) 322-331. [PMID: 6033450]
3. Casazza, J.P. and Fromm, H.J. Purification and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes. Biochemistry 16 (1977) 3091-3097. [PMID: 196625]
Accepted name: phosphoramidate—hexose phosphotransferase
Reaction: phosphoramidate + D-hexose = NH3 + α-D-hexose 1-phosphate
Other name(s): phosphoramidate-hexose transphosphorylase; phosphoramidic-hexose transphosphorylase; phosphoramidate:hexose 1-phosphotransferase
Systematic name: phosphoramidate:D-hexose 1-phosphotransferase
Comments: Activity is observed with several hexoses; of these glucose is the best substrate and the product from it is α-D-glucose 1-phosphate. The phosphoramidate donor can be replaced by N-phosphoglycine and by an N-phosphohistidine. May be identical with EC 3.1.3.9 glucose-6-phosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-45-2
References:
1. Smith R.A. and Thiesen, M.C. Phosphoramidate-hexose transphosphorylase. Methods Enzymol. 9 (1966) 403-407.
Accepted name: polyphosphate—glucose phosphotransferase
Reaction: (phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
Other name(s): polyphosphate glucokinase; polyphosphate-D-(+)-glucose-6-phosphotransferase; polyphosphate-glucose 6-phosphotransferase
Systematic name: polyphosphate:D-glucose 6-phosphotransferase
Comments: Requires a neutral salt, e.g. KCl, for maximum activity. Also acts on glucosamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-50-5
References:
1. Szymona, M. Purification and properties of a new hexokinase utilizing inorganic pyrophosphate. Acta Biochim. Pol. 9 (1962) 165-181.
2. Szymona, M. and Ostrowski, W. Inorganic polyphosphate glucokinase of Mycobacterium phlei. Biochim. Biophys. Acta 85 (1964) 283-295.
Accepted name: inositol 3-kinase
Reaction: ATP + myo-inositol = ADP + 1D-myo-inositol 3-phosphate
Other name(s): inositol-1-kinase (phosphorylating); myoinositol kinase; myo-inositol 1-kinase
Systematic name: ATP:myo-inositol 1-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-07-2
References:
1. English, P.D., Dietz, M. and Albersheim, P. Myoinositol kinase: partial purification and identification of product. Science 151 (1966) 198-199.
2. Loewus, M.W., Sasaki, K., Leavitt, A.C., Muscell, L., Sherman, W.R. and Loewus, F.A. Enantiomeric form of myo-inositol-1-phosphate produced by myo-inositol-1-phosphate synthase and myoinositol kinase in higher-plants. Plant Physiol. 70 (1982) 1661-1663.
3.Stephens, L.R., Kay, R.R. and Irvine, R.F. A myo-inositol D-3 hydroxykinase activity in Dictyostelium. Biochem. J. 272 (1990) 201-210. [PMID: 2176081]
Accepted name: scyllo-inosamine 4-kinase
Reaction: ATP + 1-amino-1-deoxy-scyllo-inositol = ADP + 1-amino-1-deoxy-scyllo-inositol 4-phosphate
Other name(s): scyllo-inosamine kinase (phosphorylating); scyllo-inosamine kinase; ATP:inosamine phosphotransferase
Systematic name: ATP:1-amino-1-deoxy-scyllo-inositol 4-phosphotransferase
Comments: Also acts on streptamine, 2-deoxystreptamine and 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-08-3
References:
1. Walker, J.B. Enzymic reactions involved in streptomycin biosynthesis and metabolisms. Lloydia 34 (1971) 363-371.
2. Walker, J.B. and Walker, M.S. Enzymatic synthesis of streptidine from scyllo-inosamine. Biochemistry 6 (1967) 3821-3829. [PMID: 6076630]
Accepted name: undecaprenol kinase
Reaction: ATP + undecaprenol = ADP + undecaprenyl phosphate
Other name(s): isoprenoid alcohol kinase; isoprenoid alcohol phosphokinase; C55-isoprenoid alcohol phosphokinase; isoprenoid alcohol kinase (phosphorylating); C55-isoprenoid alcohol kinase; C55-isoprenyl alcohol phosphokinase; polyisoprenol kinase
Systematic name: ATP:undecaprenol phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9068-22-8
References:
1. Higashi, Y., Siewert, G. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIX. Isoprenoid alcohol phosphokinase. J. Biol. Chem. 245 (1970) 3683-3690. [PMID: 4248528]
Accepted name: 1-phosphatidylinositol 4-kinase
Reaction: ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
For diagram click here.
Other name(s): phosphatidylinositol kinase (phosphorylating); phosphatidylinositol 4-kinase; phosphatidylinositol kinase; type II phosphatidylinositol kinase; PI kinase; PI 4-kinase
Systematic name: ATP:1-phosphatidyl-1D-myo-inositol 4-phosphotransferase
Comments: This reaction is catalysed by at least two different isoforms.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37205-54-2
References:
1. Colodzin, M. and Kennedy, E.P. Biosynthesis of diphosphoinositide in brain. J. Biol. Chem. 240 (1965) 3771-3780. [PMID: 4284712]
2. Kai, M., White, G.L. and Hawthorne, J.N. The phosphatidylinositol kinase of rat brain. Biochem. J. 101 (1966) 328-337. [PMID: 4290722]
3. Walker, D.H., Dougherty, N. and Pike, L.J. Purification and characterization of a phosphatidylinositol kinase from A431 cells. Biochemistry 27 (1988) 6504-6511. [PMID: 2851325]
4. Whitman, M., Downes, C.P., Keeler, M., Keller, T. and Cantley, L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332 (1988) 644-646. [PMID: 2833705]
5. Barylko, B., Gerber, S.H., Binns, D.D., Grichine, N., Khvotchev, M., Sudhof, T.C. and Albanesi, J.P. A novel family of phosphatidylinositol 4-kinases conserved from yeast to humans. J. Biol. Chem. 276 (2001) 7705-7708. [PMID: 11244087]
Accepted name: 1-phosphatidylinositol-4-phosphate 5-kinase
Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
For diagram click here.
Other name(s): diphosphoinositide kinase; PIP kinase; phosphatidylinositol 4-phosphate kinase; phosphatidylinositol-4-phosphate 5-kinase; type I PIP kinase
Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase
Comments: This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 104645-76-3
References:
1. Kai, M., Salway, J.G. and Hawthorne, J.N. The diphosphoinositide kinase of rat brain. Biochem. J. 106 (1968) 791-801. [PMID: 4295336]
2. Kai, M., Salway, J.G., Michell, R.H. and Hawthorne, J.N. The biosynthesis of triphosphoinositide by rat brain in vitro. Biochem. Biophys. Res. Commun. 22 (1966) 370-375.
3. Rameh, L.E., Tolias, K.F., Duckworth, B.C. and Cantley, L.C. A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 390 (1997) 192-196. [PMID: 9367159]
[EC 2.7.1.69 Transferred entry: protein-Nπ-phosphohistidine—sugar phosphotransferase, now covered by EC 2.7.1.191 protein-Nπ-phosphohistidine—D-mannose phosphotransferase, EC 2.7.1.192 protein-Nπ-phosphohistidine—N-acetylmuramate phosphotransferase, EC 2.7.1.193 protein-Nπ-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase, EC 2.7.1.194 protein-Nπ-phosphohistidine—L-ascorbate phosphotransferase, EC 2.7.1.195 protein-Nπ-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase, EC 2.7.1.196 protein-Nπ-phosphohistidine—N,N'-diacetylchitobiose phosphotransferase, EC 2.7.1.197 protein-Nπ-phosphohistidine—D-mannitol phosphotransferase, EC 2.7.1.198 protein-Nπ-phosphohistidine—D-sorbitol phosphotransferase, EC 2.7.1.199 protein-Nπ-phosphohistidine—D-glucose phosphotransferase, EC 2.7.1.200 protein-Nπ-phosphohistidine—galactitol phosphotransferase, EC 2.7.1.201 protein-Nπ-phosphohistidine—trehalose phosphotransferase, EC 2.7.1.202 protein-Nπ-phosphohistidine—D-fructose phosphotransferase, EC 2.7.1.203 protein-Nπ-phosphohistidine—D-glucosaminate phosphotransferase, EC 2.7.1.204 protein-Nπ-phosphohistidine—D-galactose phosphotransferase, EC 2.7.1.205 protein-Nπ-phosphohistidine—D-cellobiose phosphotransferase, EC 2.7.1.206 protein-Nπ-phosphohistidine—L-sorbose phosphotransferase, EC 2.7.1.207 protein-Nπ-phosphohistidine—lactose phosphotransferase and EC 2.7.1.208 protein-Nπ-phosphohistidine—maltose phosphotransferase. (EC 2.7.1.69 created 1972, modified 2000, deleted 2016)]
[EC 2.7.1.70 Deleted entry: protamine kinase. This enzyme is not dependent on cAMP as was thought and is therefore identical to EC 2.7.1.37, protein kinase. (EC 2.7.1.70 created 1972, deleted 2004)]
Accepted name: shikimate kinase
Reaction: ATP + shikimate = ADP + 3-phosphoshikimate
For diagram click here.
Other name(s): shikimate kinase (phosphorylating); shikimate kinase II
Systematic name: ATP:shikimate 3-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-51-0
References:
1. Morell, H. and Sprinson, D.B. Shikimate kinase isoenzymes in Salmonella typhimurium. J. Biol. Chem. 243 (1968) 676-677. [PMID: 4866525]
Accepted name: streptomycin 6-kinase
Reaction: ATP + streptomycin = ADP + streptomycin 6-phosphate
Other name(s): streptidine kinase; SM 6-kinase; streptomycin 6-kinase (phosphorylating); streptidine kinase (phosphorylating); streptomycin 6-O-phosphotransferase; streptomycin 6-phosphotransferase
Systematic name: ATP:streptomycin 6-phosphotransferase
Comments: dATP can replace ATP; and dihydrostreptomycin, streptidine and
2-deoxystreptidine can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-11-8
References:
1. Walker, J.B. and Skorvaga, M. Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives. J. Biol. Chem. 248 (1973) 2435-2440. [PMID: 4121456]
2. Walker, J.B. and Walker, M.S. Streptomycin biosynthesis. Enzymatic synthesis of O-phosphorylstreptidine from streptidine and adenosinetriphosphate. Biochim. Biophys. Acta 148 (1967) 335-341. [PMID: 6075410]
Accepted name: inosine kinase
Reaction: ATP + inosine = ADP + IMP
Other name(s): inosine-guanosine kinase; inosine kinase (phosphorylating)
Systematic name: ATP:inosine 5'-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37237-46-0
References:
1. Pierre, K.J. and LePage, G.A. Formation of inosine-5'-monophosphate by a kinase in cell-free extracts of Ehrlich ascites cells in vitro. Proc. Soc. Exp. Biol. Med. 127 (1968) 432-440. [PMID: 5645030]
Accepted name: deoxycytidine kinase
Reaction: NTP + deoxycytidine = NDP + dCMP
Other name(s): deoxycytidine kinase (phosphorylating); 2'-deoxycytidine kinase; Ara-C kinase; arabinofuranosylcytosine kinase; deoxycytidine-cytidine kinase
Systematic name: NTP:deoxycytidine 5'-phosphotransferase
Comments: Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9039-45-6
References:
1. Durham, J.P. and Ives, D.H. Deoxycytidine kinase. II. Purification and general properties of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2276-2284. [PMID: 5442271]
2. Ives, D.H. and Durham, J.P. Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2285-2294. [PMID: 5462538]
3. Kessel, D. Properties of deoxycytidine kinase partially purified from L1210 cells. J. Biol. Chem. 243 (1968) 4739-4744.
4. Momparler, R.L. and Fischer, G.A. Mammalian deoxynucleoside kinase. I. Deoxycytidine kinase: purification, properties, and kinetic studies with cytosine arabinoside. J. Biol. Chem. 243 (1968) 4298-4304. [PMID: 5684726]
[EC 2.7.1.75 Deleted entry: thymidine kinase. Now EC 2.7.1.21 thymidine kinase (EC 2.7.1.75 created 1972, deleted 1976)]
Accepted name: 2'-deoxyadenosine kinase
Reaction: ATP + 2'-deoxyadenosine = ADP + dAMP
Other name(s): purine-deoxyribonucleoside kinase
deoxyadenosine kinase (phosphorylating) (ambiguous); purine-deoxyribonucleoside kinase (ambiguous); deoxyadenosine kinase (ambiguous); ATP:deoxyadenosine 5'-phosphotransferase (ambiguous)
Systematic name: ATP:2'-deoxyadenosine 5'-phosphotransferase
Comments: 2'-Deoxyguanosine can also act as acceptor. Possibly identical with EC 2.7.1.74 deoxycytidine kinase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-12-9
References:
1. Chang, C.H., Brockman, R.W. and Bennett, L.L., Jr. Purification and some properties of a deoxyribonucleoside kinase from L1210 cells. Cancer Res. 42 (1982) 3033-3039. [PMID: 6284353]
2. Krygier, V. and Momparler, R.L. The regulatory properties of deoxyadenosine kinase. Biochim. Biophys. Acta 161 (1968) 578-580. [PMID: 5667299]
Accepted name: nucleoside phosphotransferase
Reaction: a nucleotide + a 2'-deoxyribonucleoside = a nucleoside + a 2'-deoxyribonucleoside 5'-phosphate
Other name(s): nonspecific nucleoside phosphotransferase; nucleotide:3'-deoxynucleoside 5'-phosphotransferase
Systematic name: nucleotide:nucleoside 5'-phosphotransferase
Comments: Phenyl phosphate and nucleoside 3'-phosphates can act as donors, although not so well as nucleoside 5'-phosphates. Nucleosides as well as 2'-deoxyribonucleosides can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9055-37-2
References:
1. Brunngraber, E.F. and Chargaff, E. Purification and properties of a nucleoside phosphotransferase from carrot. J. Biol. Chem. 242 (1967) 4834-4840. [PMID: 6061424]
2. Prasher, D.C., Carr, M.C., Ives, D.H., Tsai, T.-C. and Frey, P.A. Nucleoside phosphotransferase from barley. Characterization and evidence for ping pong kinetics involving phosphoryl enzyme. J. Biol. Chem. 257 (1982) 4931-4939. [PMID: 6279651]
Accepted name: polynucleotide 5'-hydroxyl-kinase
Reaction: ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA
Other name(s): ATP:5'-dephosphopolynucleotide 5'-phosphatase; PNK; polynucleotide 5'-hydroxyl kinase (phosphorylating); 5'-hydroxyl polynucleotide kinase; 5'-hydroxyl polyribonucleotide kinase; 5'-hydroxyl RNA kinase; DNA 5'-hydroxyl kinase; DNA kinase; polynucleotide kinase; polynucleotide 5'-hydroxy-kinase
Systematic name: ATP:5'-dephosphopolynucleotide 5'-phosphotransferase
Comments: Also acts on 5'-dephospho-RNA 3'-mononucleotides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37211-65-7
References:
1. Novogrodsky, A. and Hurwitz, J. The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. I. Phosphorylation at 5'-hydroxyl termini. J. Biol. Chem. 241 (1966) 2923-2932. [PMID: 4287929]
2. Novogrodsky, A., Tal, M., Traub, A. and Hurwitz, J. The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. II. Further properties of the 5'-hydroxyl polynucleotide kinase. J. Biol. Chem. 241 (1966) 2933-2943. [PMID: 4287930]
Accepted name: diphosphate—glycerol phosphotransferase
Reaction: diphosphate + glycerol = phosphate + glycerol 1-phosphate
Other name(s): PPi-glycerol phosphotransferase; pyrophosphate-glycerol phosphotransferase
Systematic name: diphosphate:glycerol 1-phosphotransferase
Comments: May be identical with EC 3.1.3.9 glucose-6-phosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-13-0
References:
1. Stetten, M.R. Enzymatic synthesis of glycerol I-phosphate. Elevation in diabetic and fasted animals, compared with glucose-6-phosphatase and related enzyme activities. Biochim. Biophys. Acta 208 (1970) 394-403. [PMID: 4319153]
Accepted name: diphosphate—serine phosphotransferase
Reaction: diphosphate + L-serine = phosphate + O-phospho-L-serine
For diagram of reaction click here.
Other name(s): pyrophosphate-serine phosphotransferase; pyrophosphate-L-serine phosphotransferase
Systematic name: diphosphate:L-serine O-phosphotransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37205-58-6
References:
1. Cagen, L.M. and Friedmann, H.C. Enzymatic phosphorylation of serine. J. Biol. Chem. 247 (1972) 3382-3392. [PMID: 4337852]
Accepted name: hydroxylysine kinase
Reaction: GTP + 5-hydroxy-L-lysine = GDP + 5-phosphooxy-L-lysine
Other name(s): hydroxylysine kinase (phosphorylating); guanosine triphosphate:5-hydroxy-L-lysine O-phosphotransferase
Systematic name: GTP:5-hydroxy-L-lysine O-phosphotransferase
Comments: Both the natural 5-hydroxy-L-lysine and its 5-epimer act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9073-58-9
References:
1. Hiles, R.A. and Henderson, L.M. The partial purification and properties of hydroxylysine kinase from rat liver. J. Biol. Chem. 247 (1972) 646-651. [PMID: 4621658]
Accepted name: ethanolamine kinase
Reaction: ATP + ethanolamine = ADP + O-phosphoethanolamine
Other name(s): ethanolamine kinase (phosphorylating); ethanolamine phosphokinase
Systematic name: ATP:ethanolamine O-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9075-78-9
References:
1. Faulkner, A. and Turner, J.M. Phosphorylation of ethanolamine in catabolism: biodegradative adenosine triphosphate-ethanolamine phosphotransferase and related enzymes in bacteria. Biochem. Soc. Trans. 2 (1974) 133-136.
2. Sung, C.-P. and Johnstone, R.M. Phosphorylation of choline and ethanolamine in Ehrlich ascites-carcinoma cells. Biochem. J. 105 (1967) 497-503. [PMID: 5626092]
3. Weinhold, P.A. and Rethy, V.B. Ethanolamine phosphokinase: activity and properties during liver development. Biochim. Biophys. Acta 276 (1972) 143-154. [PMID: 5047700]
Accepted name: pseudouridine kinase
Reaction: ATP + pseudouridine = ADP + pseudouridine 5'-phosphate
Other name(s): pseudouridine kinase (phosphorylating)
Systematic name: ATP:pseudouridine 5'-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-40-5
References:
1. Solomon, L.R. and Breitman, T.R. Pseudouridine kinase of Escherichia coli: a new enzyme. Biochem. Biophys. Res. Commun. 44 (1971) 299-304. [PMID: 4334133]
Accepted name: alkylglycerone kinase
Reaction: ATP + O-alkylglycerone = ADP + O-alkylglycerone phosphate
Other name(s): alkyldihydroxyacetone kinase (phosphorylating); alkyldihydroxyacetone kinase
Systematic name: ATP:O-alkylglycerone phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52227-80-2
References:
1. Chae, K., Piantadosi, C. and Snyder, F. Reductase, phosphatase, and kinase activities in the metabolism of alkyldihydroxyacetone phosphate and alkyldihydroxyacetone. J. Biol. Chem. 248 (1973) 6718-6723. [PMID: 4147653]
Accepted name: β-glucoside kinase
Reaction: ATP + cellobiose = ADP + 6-phospho-β-D-glucosyl-(1→4)-D-glucose
Other name(s): β-D-glucoside kinase (phosphorylating)
Systematic name: ATP:cellobiose 6-phosphotransferase
Comments: Phosphorylates a number of β-D-glucosides; GTP, CTP, ITP and UTP can also act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37205-53-1
References:
1. Palmer, R.E. and Anderson, R.L. Cellobiose metabolism in Aerobacter aerogenes. II. Phosphorylation of cellobiose with adenosine 5'-triphosphate by a β-glucoside kinase. J. Biol. Chem. 247 (1972) 3415-3419. [PMID: 5030625]
Accepted name: NADH kinase
Reaction: ATP + NADH = ADP + NADPH
Other name(s): reduced nicotinamide adenine dinucleotide kinase (phosphorylating); DPNH kinase; reduced diphosphopyridine nucleotide kinase; NADH2 kinase
Systematic name: ATP:NADH 2'-phosphotransferase
Comments: CTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing order of activity). The enzyme is specific for NADH. Activated by acetate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-39-2
References:
1. Griffiths, M.M. and Bernofsky, C. Purification and properties of reduced diphosphopyridine nucleotide kinase from yeast mitochondria. J. Biol. Chem. 247 (1972) 1473-1478. [PMID: 4335000]
Accepted name: streptomycin 3"-kinase
Reaction: ATP + streptomycin = ADP + streptomycin 3"-phosphate
Other name(s): streptomycin 3"-kinase (phosphorylating); streptomycin 3"-phosphotransferase
Systematic name: ATP:streptomycin 3"-phosphotransferase
Comments: Also phosphorylates dihydrostreptomycin, 3'-deoxydihydrostreptomycin and their 6-phosphates.
Links to other databases: BRENDA, EXPASY, KEMetacyc, CAS registry number: 39391-15-6
References:
1. Walker, J.B. and Skorvaga, M. Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives. J. Biol. Chem. 248 (1973) 2435-2440. [PMID: 4121456]
Accepted name: dihydrostreptomycin-6-phosphate 3'α-kinase
Reaction: ATP + dihydrostreptomycin 6-phosphate = ADP + dihydrostreptomycin 3'α,6-bisphosphate
Other name(s): dihydrostreptomycin 6-phosphate kinase (phosphorylating); ATP:dihydrostreptomycin-6-P 3'α-phosphotransferase
Systematic name: ATP:dihydrostreptomycin-6-phosphate 3'α-phosphotransferase
Comments: 3'-Deoxydihydrostreptomycin 6-phosphate can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39391-14-5
References:
1. Walker, J.B. and Skorvaga, M. Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives. J. Biol. Chem. 248 (1973) 2435-2440. [PMID: 4121456]
Accepted name: thiamine kinase
Reaction: ATP + thiamine = ADP + thiamine phosphate
Other name(s): thiamin kinase (phosphorylating); thiamin phosphokinase; ATP:thiamin phosphotransferase; thiamin kinase
Systematic name: ATP:thiamine phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-38-1
References:
1. Iwashima, A., Nishino, H. and Nose, Y. Conversion of thiamine to thiamine monophosphate by cell-free extracts of Escherichia coli. Biochim. Biophys. Acta 258 (1972) 333-337. [PMID: 4550803]
Accepted name: diphosphate—fructose-6-phosphate 1-phosphotransferase
Reaction: diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate
For diagram of reaction click here.
Other name(s): 6-phosphofructokinase (pyrophosphate); pyrophosphate-fructose 6-phosphate 1-phosphotransferase; inorganic pyrophosphate-dependent phosphofructokinase; inorganic pyrophosphate-phosphofructokinase; pyrophosphate-dependent phosphofructo-1-kinase; pyrophosphate-fructose 6-phosphate phosphotransferase
Systematic name: diphosphate:D-fructose-6-phosphate 1-phosphotransferase
Comments: The enzyme catalyses a similar reaction to EC 2.7.1.11, 6-phosphofructokinase, but utilizes diphosphate instead of ATP as the the phosphate donor. It has been described in higher plants, primitive eukaryotes, bacteria, and archaea.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 55326-40-4
References:
1. Reeves, R.E., Serrano, R. and South, D.J. 6-Phosphofructokinase (pyrophosphate). Properties of the enzyme from Entamoeba histolytica and its reaction mechanism. J. Biol. Chem. 251 (1976) 2958-2962. [PMID: 178659]
2. Reeves, R.E., South, D.J., Blytt, H.J. and Warren, L.G. Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase. A new enzyme with the glycolytic function of 6-phosphofructokinase. J. Biol. Chem. 249 (1974) 7737-7741. [PMID: 4372217]
3. Carlisle, S.M., Blakeley, S.D., Hemmingsen, S.M., Trevanion, S.J., Hiyoshi, T., Kruger, N.J. and Dennis, D.T. Pyrophosphate-dependent phosphofructokinase. Conservation of protein sequence between the α- and β-subunits and with the ATP-dependent phosphofructokinase. J. Biol. Chem. 265 (1990) 18366-18371. [PMID: 2170409]
4. Ladror, U.S., Gollapudi, L., Tripathi, R.L., Latshaw, S.P. and Kemp, R.G. Cloning, sequencing, and expression of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii. J. Biol. Chem. 266 (1991) 16550-16555. [PMID: 1653240]
5. Siebers, B., Klenk, H.P. and Hensel, R. PPi-dependent phosphofructokinase from Thermoproteus tenax, an archaeal descendant of an ancient line in phosphofructokinase evolution. J. Bacteriol. 180 (1998) 2137-2143. [PMID: 9555897]
Accepted name: sphingosine kinase
Reaction: ATP + a sphingoid base = ADP + a sphingoid base 1-phosphate
Other name(s): SPHK1 (gene name); SPHK2 (gene name); dihydrosphingosine kinase; dihydrosphingosine kinase (phosphorylating); sphingosine kinase (phosphorylating); sphingoid base kinase; sphinganine kinase; ATP:sphinganine 1-phosphotransferase
Systematic name: ATP:sphingoid base 1-phosphotransferase
Comments: The enzyme is involved in the production of sphingolipid metabolites. It phosphorylates various sphingoid long-chain bases, such as sphingosine, D-erythro-dihydrosphingosine (sphinganine), phytosphingosine (4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine and D-threo-dihydrosphingosine and L-threo-dihydrosphingosine. The exact substrate range depends on the species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50864-48-7
References:
1. Stoffel, W., Heimann, G. and Hellenbroich, B. Sphingosine kinase in blood platelets. Hoppe-Seyler's Z. Physiol. Chem. 354 (1973) 562-566. [PMID: 4372149]
2. Stoffel, W., Bauer, E. and Stahl, J. The metabolism of sphingosine bases in Tetrahymena pyriformis. Sphingosine kinase and sphingosine-1-phosphate lyase. Hoppe-Seyler's Z. Physiol. Chem. 355 (1974) 61-74. [PMID: 4373374]
3. Nagiec, M.M., Skrzypek, M., Nagiec, E.E., Lester, R.L. and Dickson, R.C. The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases. J. Biol. Chem. 273 (1998) 19437-19442. [PMID: 9677363]
4. Kohama, T., Olivera, A., Edsall, L., Nagiec, M.M., Dickson, R. and Spiegel, S. Molecular cloning and functional characterization of murine sphingosine kinase. J. Biol. Chem. 273 (1998) 23722-23728. [PMID: 9726979]
5. Liu, H., Sugiura, M., Nava, V.E., Edsall, L.C., Kono, K., Poulton, S., Milstien, S., Kohama, T. and Spiegel, S. Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform. J. Biol. Chem. 275 (2000) 19513-19520. [PMID: 10751414]
6. Worrall, D., Liang, Y.K., Alvarez, S., Holroyd, G.H., Spiegel, S., Panagopulos, M., Gray, J.E. and Hetherington, A.M. Involvement of sphingosine kinase in plant cell signalling. Plant J. 56 (2008) 64-72. [PMID: 18557834]
Accepted name: 5-dehydro-2-deoxygluconokinase
Reaction: ATP + 5-dehydro-2-deoxy-D-gluconate = ADP + 6-phospho-5-dehydro-2-deoxy-D-gluconate
For diagram of reaction click here.
Other name(s): 5-keto-2-deoxygluconokinase; 5-keto-2-deoxyglucono kinase (phosphorylating); DKH kinase
Systematic name: ATP:5-dehydro-2-deoxy-D-gluconate 6-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-35-8
References:
1. Anderson, W.A. and Magasanik, B. The pathway of myo-inositol degradation in Aerobacter aerogenes. Conversion of 2-deoxy-5-keto-D-gluconic acid to glycolytic intermediates. J. Biol. Chem. 246 (1971) 5662-5675. [PMID: 4328832]
Accepted name: alkylglycerol kinase
Reaction: ATP + 1-O-alkyl-sn-glycerol = ADP + 1-O-alkyl-sn-glycerol 3-phosphate
Other name(s): 1-alkylglycerol kinase (phosphorylating); ATP-alkylglycerol phosphotransferase; alkylglycerol phosphotransferase; ATP: 1-alkyl-sn-glycerol phosphotransferase
Systematic name: ATP:1-O-alkyl-sn-glycerol 3-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 55354-37-5
References:
1. Rock, C.O. and Snyder, F. Biosynthesis of 1-alkyl-sn-glycero-3-phosphate via adenosine triphosphate:1-alkyl-sn-glycerol phosphotransferase. J. Biol. Chem. 249 (1974) 5382-5387. [PMID: 4369816]
Accepted name: acylglycerol kinase
Reaction: ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate
Other name(s): monoacylglycerol kinase; monoacylglycerol kinase (phosphorylating); sn-2-monoacylglycerol kinase; MGK; monoglyceride kinase; monoglyceride phosphokinase
Systematic name: ATP:acylglycerol 3-phosphotransferase
Comments: Acts on both 1- and 2-acylglycerols.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-37-0
References:
1. Pieringer, R.A. and Hokin, L.E. Biosynthesis of lysophosphatidic acid from monoglyceride and adenosine triphosphate. J. Biol. Chem. 237 (1962) 653-658.
2. Pieringer, R.A. and Kunnes, R.S. The biosynthesis of phosphatidic acid and lysophosphatidic acid by glyceride phosphokinase pathways in Escherichia coli. J. Biol. Chem. 240 (1965) 2833-2838.
Accepted name: kanamycin kinase
Reaction: ATP + kanamycin = ADP + kanamycin 3'-phosphate
Glossary: kanamycin
Other name(s): neomycin-kanamycin phosphotransferase;
kanamycin kinase (phosphorylating); neomycin phosphotransferase
Systematic name: ATP:kanamycin 3'-O-phosphotransferase
Comments: Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A. An enzyme from Pseudomonas aeruginosa also acts on butirosin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-36-9
References:
1. Doi, O., Ogura, M., Tanaka, N. and Umezawa, H. Inactivation of kanamycin, neomycin, and streptomycin by enzymes obtained in cells of Pseudomonas aeruginosa. Appl. Microbiol. 16 (1968) 1276-1281. [PMID: 4970990]
2. Dolin, M.I. The Streptococcus faecalis oxidases for reduced diphosphopyridine nucleotide. III. Isolation and properties of a flavin peroxidase for reduced diphosphopyridine nucleotide. J. Biol. Chem. 225 (1957) 557-573.
[EC 2.7.1.96 Deleted entry: NADH kinase. Now included with EC 2.7.1.86 NADH kinase (EC 2.7.1.96 created 1978, deleted 1978)]
[EC 2.7.1.97 Deleted entry: identical with EC 2.7.1.125 rhodopsin kinase (EC 2.7.1.97 created 1978, deleted 1992)]
[EC 2.7.1.98 Deleted entry: phosphoenolpyruvate—fructose phosphotransferase (EC 2.7.1.98 created 1978, deleted 1984)]
[EC 2.7.1.99 Transferred entry: now EC 2.7.11.2, [pyruvate dehydrogenase (acetyl-transferring)] kinase (EC 2.7.1.99 created 1978, deleted 2005)]
Accepted name: S-methyl-5-thioribose kinase
Reaction: ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-α-D-ribose 1-phosphate
For diagram click here.
Other name(s): 5-methylthioribose kinase (phosphorylating); methylthioribose kinase; 5-methylthioribose kinase; ATP:S5-methyl-5-thio-D-ribose 1-phosphotransferase
Systematic name: ATP:S-methylmethyl-5-thio-D-ribose 1-phosphotransferase
Comments: CTP also acts, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68247-56-3
References:
1. Ferro, A.J., Barrett, A. and Shapiro, S.K. 5-Methylthioribose kinase. A new enzyme involved in the formation of methionine from 5-methylthioribose. J. Biol. Chem. 253 (1978) 6021-6025. [PMID: 210167]
2. Guranowski, A. Plant 5-methylthioribose kinase. Plant Physiol. 71 (1983) 932-935.