See separate file for EC 2.7.1.101 to EC 2.7.1.172.
Continued with:
EC 2.7.1.101 to EC 2.7.1.172
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, 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, 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, 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
Other name(s): D-arabinokinase (phosphorylating)
Systematic name: ATP:D-arabinose 5-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, 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, 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, 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-D-galactonate 6-phosphate
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, 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, 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
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, 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, 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, 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, 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, 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, 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, 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, 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, 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]
Accepted name: protein-Nπ-phosphohistidine—sugar phosphotransferase
Reaction: protein Nπ-phospho-L-histidine + sugar = protein histidine + sugar phosphate
Other name(s): glucose permease; PTS permease; phosphotransferase, phosphohistidinoprotein-hexose; enzyme IIl4ac; gene glC proteins; gene bglC RNA formation factors; PEP-dependent phosphotransferase enzyme II; PEP-sugar phosphotransferase enzyme II; phosphoenolpyruvate-sugar phosphotransferase enzyme II; phosphohistidinoprotein-hexose phosphotransferase; phosphohistidinoprotein-hexose phosphoribosyltransferase; phosphoprotein factor-hexose phosophotransferase; protein, specific or class, gene bglC; ribonucleic acid formation factor, gene glC; sucrose phosphotransferase system II; protein-Nπ-phosphohistidine:sugar N-pros-phosphotransferase; protein-Nπ-phosphohistidine:sugar Nπ-phosphotransferase
Systematic name: protein-Nπ-phospho-L-histidine:sugar Nπ-phosphotransferase
Comments: Enzyme II of the phosphotransferase system. Comprises a group of related enzymes. The protein substrate is a phosphocarrier protein of low molecular mass (9.5 kDa). The protein is phosphorylated in a reaction catalysed by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase) and this acts as the phosphate donor for the above reaction. The enzyme translocates the sugar it phosphorylates into bacteria. Aldohexoses, and their glycosides and alditols, are phosphorylated on O-6, whereas fructose and sorbose are phosphorylated on O-1. Glycerone and disaccharides are also substrates.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37278-09-4
References:
1. Kornberg, H.L. and Riordan, C. Uptake of galactose into Escherichia coli by facilitated diffusion. J. Gen. Microbiol. 94 (1976) 75-89. [PMID: 778334]
2. Postma, P.W. and Roseman, S. The bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochim. Biophys. Acta 457 (1976) 213-257. [PMID: 187249]
[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, 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, 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, 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, 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: deoxyadenosine kinase
Reaction: ATP + deoxyadenosine = ADP + dAMP
Other name(s): purine-deoxyribonucleoside kinase
deoxyadenosine kinase (phosphorylating); purine-deoxyribonucleoside kinase
Systematic name: ATP:deoxyadenosine 5'-phosphotransferase
Comments: Deoxyguanosine can also act as acceptor. Possibly identical with EC 2.7.1.74 deoxycytidine kinase.
Links to other databases: BRENDA, EXPASY, KEGG, 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'-deoxynucleoside = a nucleoside + a 2'-deoxynucleoside 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'-deoxynucleosides can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, 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, 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, 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
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, 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-phosphonooxy-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, 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, 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, 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, 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 = 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, 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, 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, KEGG, 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, 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, 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
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
Links to other databases: BRENDA, EXPASY, GTD, KEGG, 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]
Accepted name: sphinganine kinase
Reaction: ATP + sphinganine = ADP + sphinganine 1-phosphate
Other name(s): dihydrosphingosine kinase; dihydrosphingosine kinase (phosphorylating); sphingosine kinase (phosphorylating)
Systematic name: ATP:sphinganine 1-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 50864-48-7
References:
1. 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]
2. Stoffel, W., Heimann, G. and Hellenbroich, B. Sphingosine kinase in blood platelets. Hoppe-Seyler's Z. Physiol. Chem. 354 (1973) 562-566. [PMID: 4372149]
Accepted name: 5-dehydro-2-deoxygluconokinase
Reaction: ATP + 5-dehydro-2-deoxy-D-gluconate = ADP + 6-phospho-5-dehydro-2-deoxy-D-gluconate
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, 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, 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, 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, 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, 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.