EC |
2.7.1.1 |
Accepted name: |
hexokinase |
Reaction: |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
Other name(s): |
hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase |
Systematic name: |
ATP:D-hexose 6-phosphotransferase |
Comments: |
D-Glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-51-8 |
References: |
1. |
Bailey, K. and Webb, E.C. Purification of yeast hexokinase and its reaction with ββ′-dichlorodiethyl sulphide. Biochem. J. 42 (1948) 60–68. [PMID: 16748250] |
2. |
Berger, L., Slein, M.W., Colowick, S.P. and Cori, C.F. Isolation of hexokinase from baker's yeast. J. Gen. Physiol. 29 (1946) 379–391. [PMID: 19873467] |
3. |
Kunitz, M. and McDonald, M.R. Crystalline hexokinase (heterophosphatase). Method of isolation and properties. J. Gen. Physiol. 29 (1946) 393–412. [PMID: 19873468] |
4. |
Pollard-Knight, D. and Cornish-Bowden, A. Mechanism of liver glucokinase. Mol. Cell. Biochem. 44 (1982) 71–80. [PMID: 7048063] |
5. |
Ureta, T., Radojkovic, J., Lagos, R., Guixe, V. and Núñnez, L. Phylogenetic and ontogenetic studies of glucose phosphorylating isozymes of vertebrates. Arch. Biol. Med. Exp. 12 (1979) 587–604. [PMID: 233226] |
6. |
Cárdenas, M.L., Rabajille, E. and Niemeyer, H. Fructose: A good substrate for rat-liver 'glucokinase' (hexokinase D). Biochem. J. 222 (1984) 363–370. [PMID: 6477520] |
|
[EC 2.7.1.1 created 1961] |
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|
EC |
2.7.1.2 |
Accepted name: |
glucokinase |
Reaction: |
ATP + D-glucose = ADP + D-glucose 6-phosphate |
Other name(s): |
glucokinase (phosphorylating) |
Systematic name: |
ATP:D-glucose 6-phosphotransferase |
Comments: |
A group of enzymes found in invertebrates and microorganisms that are highly specific for glucose. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9001-36-9 |
References: |
1. |
Baumann, P. Glucokinase of Dictyostelium discoideum. Biochemistry 8 (1969) 5011–5015. [PMID: 4312464] |
2. |
Bueding, E. and MacKinnon, J.A. Hexokinases of Schistosoma mansoni. J. Biol. Chem. 215 (1955) 495–506. [PMID: 13242546] |
3. |
Porter, E.V., Chassy, B.M. and Holmlund, C.E. Purification and kinetic characterization of a specific glucokinase from Streptococcus mutans OMZ70 cells. Biochim. Biophys. Acta 709 (1982) 178–186. [DOI] [PMID: 7150605] |
|
[EC 2.7.1.2 created 1961] |
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|
EC |
2.7.1.3 |
Accepted name: |
ketohexokinase |
Reaction: |
ATP + D-fructose = ADP + D-fructose 1-phosphate |
Other name(s): |
ketohexokinase (phosphorylating) |
Systematic name: |
ATP:D-fructose 1-phosphotransferase |
Comments: |
D-Sorbose, D-tagatose and 5-dehydro-D-fructose and a number of other ketoses and their analogues can also act as substrates [4]. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-50-6 |
References: |
1. |
Cori, G.T., Ochoa, S., Slein, M.W. and Cori, C.F. The metabolism of fructose in liver. Isolation of fructose-1-phosphate and inorganic pyrophosphate. Biochim. Biophys. Acta 7 (1951) 304–317. [PMID: 14858418] |
2. |
Hers, H.G. La fructokinase du foie. Biochim. Biophys. Acta 8 (1952) 416–423. [PMID: 13208667] |
3. |
Parks, R.E., Ben-Gershom, E. and Lardy, H.A. Liver fructokinase. J. Biol. Chem. 227 (1957) 231–242. [PMID: 13449068] |
4. |
Raushel, F.M. and Cleland, W.W. Bovine liver fructokinase: purification and kinetic properties. Biochemistry 16 (1977) 2169–2175. [PMID: 193556] |
|
[EC 2.7.1.3 created 1961] |
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|
EC |
2.7.1.4 |
Accepted name: |
fructokinase |
Reaction: |
ATP + D-fructose = ADP + D-fructose 6-phosphate |
Other name(s): |
fructokinase (phosphorylating); D-fructokinase; D-fructose(D-mannose)kinase |
Systematic name: |
ATP:D-fructose 6-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-51-7 |
References: |
1. |
Bueding, E. and MacKinnon, J.A. Hexokinases of Schistosoma mansoni. J. Biol. Chem. 215 (1955) 495–506. [PMID: 13242546] |
2. |
Medina, A. and Sols, A. A specific fructokinase in peas. Biochim. Biophys. Acta 19 (1956) 378–379. [DOI] [PMID: 13315288] |
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[EC 2.7.1.4 created 1961] |
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|
EC |
2.7.1.5 |
Accepted name: |
rhamnulokinase |
Reaction: |
ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate |
|
For diagram of L-Rhamnose metabolism, click here |
Other name(s): |
RhuK; rhamnulokinase (phosphorylating); L-rhamnulokinase; L-rhamnulose kinase; rhamnulose kinase |
Systematic name: |
ATP:L-rhamnulose 1-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-52-8 |
References: |
1. |
Wilson, D.M. and Ajl, S. Metabolism of L-rhamnose by Escherichia coli. II. The phosphorylation of L-rhamnulose. J. Bacteriol. 73 (1957) 415–420. [PMID: 13416205] |
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[EC 2.7.1.5 created 1961] |
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EC |
2.7.1.6 |
Accepted name: |
galactokinase |
Reaction: |
ATP + α-D-galactose = ADP + α-D-galactose 1-phosphate |
Other name(s): |
galactokinase (phosphorylating); ATP:D-galactose-1-phosphotransferase |
Systematic name: |
ATP:α-D-galactose 1-phosphotransferase |
Comments: |
Part of the Leloir pathway for galactose metabolism. The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-α-D-galactosamine [4-6]. |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-53-9 |
References: |
1. |
Cardini, C.E. and Leloir, L.F. Enzymic phosphorylation of galactosamine and galactose. Arch. Biochem. Biophys. 45 (1953) 55–64. [DOI] [PMID: 13058412] |
2. |
Neufeld, E.F., Feingold, D.S. and Hassid, W.Z. Phosphorylation of D-galactose and L-arabinose by extracts from Phaseolus aureus seedlings. J. Biol. Chem. 235 (1960) 906–909. [PMID: 14426659] |
3. |
Wilkinson, J.F. The pathway of the adaptive fermentation of galactose by yeast. Biochem. J. 44 (1949) 460–467. [PMID: 16748546] |
4. |
Yang, J., Fu, X., Jia, Q., Shen, J., Biggins, J.B., Jiang, J., Zhao, J., Schmidt, J.J., Wang, P.G. and Thorson, J.S. Studies on the substrate specificity of Escherichia coli galactokinase. Org. Lett. 5 (2003) 2223–2226. [DOI] [PMID: 12816414] |
5. |
Timson, D.J. and Reece, R.J. Sugar recognition by human galactokinase. BMC Biochem. 4:16 (2003). [DOI] [PMID: 14596685] |
6. |
Thoden, J.B., Timson, D.J., Reece, R.J. and Holden, H.M. Molecular structure of human galactokinase: implications for type II galactosemia. J. Biol. Chem. 280 (2005) 9662–9670. [DOI] [PMID: 15590630] |
|
[EC 2.7.1.6 created 1961] |
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|
EC |
2.7.1.7 |
Accepted name: |
mannokinase |
Reaction: |
ATP + D-mannose = ADP + D-mannose 6-phosphate |
Other name(s): |
mannokinase (phosphorylating); D-fructose (D-mannose) kinase |
Systematic name: |
ATP:D-mannose 6-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9030-54-0 |
References: |
1. |
Bueding, E. and MacKinnon, J.A. Hexokinases of Schistosoma mansoni. J. Biol. Chem. 215 (1955) 495–506. [PMID: 13242546] |
|
[EC 2.7.1.7 created 1961] |
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|
EC |
2.7.1.8 |
Accepted name: |
glucosamine kinase |
Reaction: |
ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate |
Glossary: |
D-glucosamine 6-phosphate = 2-amino-2-deoxy-D-glucose 6-phosphate |
Other name(s): |
glucosamine kinase (phosphorylating); ATP:2-amino-2-deoxy-D-glucose-6-phosphotransferase; aminodeoxyglucose kinase; ATP:D-glucosamine phosphotransferase |
Systematic name: |
ATP:D-glucosamine 6-phosphotransferase |
Comments: |
The enzyme is specific for glucosamine and has only a minor activity with D-glucose. Two unrelated enzymes with this activity have been described. One type was studied in the bacterium Vibrio cholerae, where it participates in a chitin degradation pathway. The other type has been described from actinobacteria, where it is involved in the incorporation of environmental glucosamine into antibiotic biosynthesis pathways. cf. EC 2.7.1.147, ADP-specific glucose/glucosamine kinase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9031-90-7 |
References: |
1. |
Bueding, E. and MacKinnon, J.A. Hexokinases of Schistosoma mansoni. J. Biol. Chem. 215 (1955) 495–506. [PMID: 13242546] |
2. |
Park, J.K., Wang, L.X. and Roseman, S. Isolation of a glucosamine-specific kinase, a unique enzyme of Vibrio cholerae. J. Biol. Chem. 277 (2002) 15573–15578. [DOI] [PMID: 11850417] |
3. |
Manso, J.A., Nunes-Costa, D., Macedo-Ribeiro, S., Empadinhas, N. and Pereira, P.J.B. Molecular fingerprints for a novel enzyme family in actinobacteria with glucosamine kinase activity. MBio 10:e00239-19 (2019). [PMID: 31088917] |
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[EC 2.7.1.8 created 1961, modified 2014, modified 2020] |
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EC
|
2.7.1.9
|
Deleted entry: | acetylaminodeoxyglucose kinase |
[EC 2.7.1.9 created 1961, deleted 1965] |
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|
EC |
2.7.1.10 |
Accepted name: |
phosphoglucokinase |
Reaction: |
ATP + α-D-glucose 1-phosphate = ADP + α-D-glucose 1,6-bisphosphate |
Other name(s): |
glucose-phosphate kinase; phosphoglucokinase (phosphorylating); ATP:D-glucose-1-phosphate 6-phosphotransferase |
Systematic name: |
ATP:α-D-glucose-1-phosphate 6-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9032-96-6 |
References: |
1. |
Paladini, A.C., Caputto, R., Leloir, L.F., Trucco, R.E. and Cardini, C.E. The enzymatic synthesis of glucose-1,6-diphosphate. Arch. Biochem. 23 (1949) 55–66. [PMID: 18135764] |
|
[EC 2.7.1.10 created 1961] |
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|
EC |
2.7.1.11 |
Accepted name: |
6-phosphofructokinase |
Reaction: |
ATP + β-D-fructofuranose 6-phosphate = ADP + β-D-fructofuranose 1,6-bisphosphate |
|
For diagram of glycolysis, click here |
Other name(s): |
phosphohexokinase; phosphofructokinase I; phosphofructokinase (phosphorylating); 6-phosphofructose 1-kinase; ATP-dependent phosphofructokinase; D-fructose-6-phosphate 1-phosphotransferase; fructose 6-phosphate kinase; fructose 6-phosphokinase; nucleotide triphosphate-dependent phosphofructokinase; phospho-1,6-fructokinase; PFK |
Systematic name: |
ATP:β-D-fructose-6-phosphate 1-phosphotransferase |
Comments: |
The enzyme from rabbit muscle displays absolute stereoselectivity for the β-anomer of D-fructofuranose 6-phosphate [9-11]. D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase. |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-80-3 |
References: |
1. |
Racker, E. Spectrophotometric measurement of hexokinase and phosphohexokinase activity. J. Biol. Chem. 167 (1947) 843–854. [PMID: 20287918] |
2. |
Axelrod, B., Saltman, P., Bandurski, R.S. and Baker, R.S. Hexokinase in higher plants. J. Biol. Chem. 197 (1952) 89–96. [PMID: 12981037] |
3. |
Ling, K.H., Pastkau, V., Marcus, F. and Lardy, H.A. Phosphofructokinase. I. Skeletal muscle. Methods Enzymol. 9 (1966) 425–429. |
4. |
Mansour, T.E. Phosphofructokinase. II. Heart muscle. Methods Enzymol. 9 (1966) 430–436. |
5. |
Parmeggiano, A., Luft, J.H., Love, D.S. and Krebs, E.G. Crystallization and properties of rabbit skeletal muscle phosphofructokinase. J. Biol. Chem. 241 (1966) 4625–4637. [PMID: 4224472] |
6. |
Sols, A. and Salas, M.L. Phosphofructokinase. III. Yeast. Methods Enzymol. 9 (1966) 436–442. |
7. |
Odeide, R., Guilloton, M., Dupuis, B., Ravon, D. and Rosenberg, A.J. Study of an enzyme allosteric to 2 substrates: phosphofructokinase of rat muscle. I. Preparation and crystallization of the enzyme. Bull. Soc. Chim. Biol. 50 (1968) 2023–2033. [PMID: 4237772] |
8. |
Uyeda, K. and Kurooka, S. Crystallization and properties of phosphofructokinase from Clostridium pasteurianum. J. Biol. Chem. 245 (1970) 3315–3324. [PMID: 4248230] |
9. |
Fishbein, R., Benkovic, P.A., Schray, K.J., Siewers, I.J., Steffens, J.J. and Benkovic, S.J. Anomeric specificity of phosphofructokinase from rabbit muscle. J. Biol. Chem. 249 (1974) 6047–6051. [PMID: 4278654] |
10. |
Wurster, B. and Hess, B. Anomeric specificity of fructose-6-phosphate kinase (EC 2.7.1.11) from rabbit muscle. FEBS Lett. 38 (1974) 257–260. [DOI] [PMID: 4277364] |
11. |
Koerner, T.A., Jr., Younathan, E.S., Ashour, A.L. and Voll, R.J. The fructose 6-phosphate site of phosphofructokinase. I. Tautomeric and anomeric specificity. J. Biol. Chem. 249 (1974) 5749–5754. [PMID: 4278316] |
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[EC 2.7.1.11 created 1961, modified 2021] |
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EC |
2.7.1.12 |
Accepted name: |
gluconokinase |
Reaction: |
ATP + D-gluconate = ADP + 6-phospho-D-gluconate |
Other name(s): |
gluconokinase (phosphorylating); gluconate kinase |
Systematic name: |
ATP:D-gluconate 6-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-55-1 |
References: |
1. |
Cohen, S.S. Gluconokinase and the oxidative path of glucose-6-phosphate utilization. J. Biol. Chem. 189 (1951) 617–628. [PMID: 14832279] |
2. |
Leder, I.G. Hog kidney gluconokinase. J. Biol. Chem. 225 (1957) 125–136. [PMID: 13416223] |
3. |
Narrod, S.A. and Wood, W.A. Carbohydrate oxidation by Pseudomonas fluorescens. V. Evidence for gluconokinase and 2-ketogluconokinase. J. Biol. Chem. 220 (1956) 45–55. [PMID: 13319325] |
4. |
Sable, H.Z. and Guarino, A.J. Phosphorylation of gluconate in yeast extracts. J. Biol. Chem. 196 (1952) 395–402. [PMID: 12980980] |
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[EC 2.7.1.12 created 1961] |
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EC |
2.7.1.13 |
Accepted name: |
dehydrogluconokinase |
Reaction: |
ATP + 2-dehydro-D-gluconate = ADP + 6-phospho-2-dehydro-D-gluconate |
Other name(s): |
ketogluconokinase; 2-ketogluconate kinase; ketogluconokinase (phosphorylating); 2-ketogluconokinase |
Systematic name: |
ATP:2-dehydro-D-gluconate 6-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9030-56-2 |
References: |
1. |
Frampton, E.W. and Wood, W.A. Purification and properties of 2-ketogluconokinase from Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 2578–2580. [PMID: 13894459] |
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[EC 2.7.1.13 created 1961] |
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EC |
2.7.1.14 |
Accepted name: |
sedoheptulokinase |
Reaction: |
ATP + sedoheptulose = ADP + sedoheptulose 7-phosphate |
Other name(s): |
heptulokinase; sedoheptulokinase (phosphorylating) |
Systematic name: |
ATP:sedoheptulose 7-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9030-63-1 |
References: |
1. |
Ebata, M., Sato, R. and Bak, T. The enzymic phosphorylation of sedoheptulose. J. Biochem. (Tokyo) 42 (1955) 715–725. |
|
[EC 2.7.1.14 created 1961] |
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EC |
2.7.1.15 |
Accepted name: |
ribokinase |
Reaction: |
ATP + D-ribose = ADP + D-ribose 5-phosphate |
Other name(s): |
deoxyribokinase; ribokinase (phosphorylating); D-ribokinase |
Systematic name: |
ATP:D-ribose 5-phosphotransferase |
Comments: |
2-Deoxy-D-ribose can also act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-84-0 |
References: |
1. |
Agranoff, B.W. and Brady, R.O. Purification and properties of calf liver ribokinase. J. Biol. Chem. 219 (1956) 221–229. [PMID: 13295274] |
2. |
Ginsburg, A. A deoxyribokinase from Lactobacillus plantarum. J. Biol. Chem. 234 (1959) 481–487. [PMID: 13641245] |
|
[EC 2.7.1.15 created 1961] |
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EC |
2.7.1.16 |
Accepted name: |
ribulokinase |
Reaction: |
ATP + L(or D)-ribulose = ADP + L(or D)-ribulose 5-phosphate |
Other name(s): |
ribulokinase (phosphorylating); L-ribulokinase |
Systematic name: |
ATP:L(or D)-ribulose 5-phosphotransferase |
Comments: |
Ribitol and L-arabinitol can also act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-57-3 |
References: |
1. |
Burma, D.P. and Horecker, B.L. Pentose fermentation by Lactobacillus plantarum. III. Ribulokinase. J. Biol. Chem. 231 (1958) 1039–1051. [PMID: 13539035] |
2. |
Lee, N. and Bendet, I. Crystalline L-ribulokinase from Escherichia coli. J. Biol. Chem. 242 (1967) 2043–2050. [PMID: 5336963] |
3. |
Simpson, F.J., Wolin, M.J. and Wood, W.A. Degradation of L-arabinose by Aerobacter aerogenes. I. A pathway involving phosphorylated intermediates. J. Biol. Chem. 230 (1958) 457–472. [PMID: 13502414] |
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[EC 2.7.1.16 created 1961] |
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EC |
2.7.1.17 |
Accepted name: |
xylulokinase |
Reaction: |
ATP + D-xylulose = ADP + D-xylulose 5-phosphate |
Other name(s): |
xylulokinase (phosphorylating); D-xylulokinase |
Systematic name: |
ATP:D-xylulose 5-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-58-4 |
References: |
1. |
Hickman, J. and Ashwell, G. Purification and properties of D-xylulokinase in liver. J. Biol. Chem. 232 (1958) 737–748. [PMID: 13549459] |
2. |
Simpson, F.J. D-Xylulokinase. Methods Enzymol. 9 (1966) 454–458. |
3. |
Slein, M.W. Xylose isomerase from Pasteurella pestis, strain A-1122. J. Am. Chem. Soc. 77 (1955) 1663–1667. [DOI] |
4. |
Stumpf, P.K. and Horecker, B.L. The røole of xylulose 5-phosphate in xylose metabolism of Lactobacillus pentosus. J. Biol. Chem. 218 (1956) 753–768. [PMID: 13295228] |
|
[EC 2.7.1.17 created 1961] |
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EC |
2.7.1.18 |
Accepted name: |
phosphoribokinase |
Reaction: |
ATP + D-ribose 5-phosphate = ADP + α-D-ribose 1,5-bisphosphate |
Other name(s): |
phosphoribokinase (phosphorylating) |
Systematic name: |
ATP:D-ribose-5-phosphate 1-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-59-5 |
References: |
1. |
Krebs, E.G. Phosphorylase b kinase from rabbit muscle. Methods Enzymol. 8 (1966) 543–546. |
2. |
Scarano, E. Quoted by H.M. Kalckar The role of phosphoglycosyl compounds in the biosynthesis of nucleosides and nucleotides. Biochim. Biophys. Acta 12 (1953) 250–264. [PMID: 13115434] |
|
[EC 2.7.1.18 created 1961] |
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EC |
2.7.1.19 |
Accepted name: |
phosphoribulokinase |
Reaction: |
ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate |
|
For diagram of the Calvin cycle, click here |
Other name(s): |
phosphopentokinase; ribulose-5-phosphate kinase; phosphopentokinase; phosphoribulokinase (phosphorylating); 5-phosphoribulose kinase; ribulose phosphate kinase; PKK; PRuK; PRK |
Systematic name: |
ATP:D-ribulose-5-phosphate 1-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-60-8 |
References: |
1. |
Hurwitz, J., Weissbach, A., Horecker, B.L. and Smyrniotis, P.Z. Spinach phosphoribulokinase. J. Biol. Chem. 218 (1956) 769–783. [PMID: 13295229] |
2. |
Jakoby, W.B., Brummond, D.O. and Ochoa, S. Formation of 3-phosphoglyceric acid by carbon dioxide fixation with spinach leaf enzymes. J. Biol. Chem. 218 (1956) 811–822. [PMID: 13295232] |
|
[EC 2.7.1.19 created 1961] |
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EC |
2.7.1.20 |
Accepted name: |
adenosine kinase |
Reaction: |
ATP + adenosine = ADP + AMP |
Other name(s): |
adenosine kinase (phosphorylating) |
Systematic name: |
ATP:adenosine 5′-phosphotransferase |
Comments: |
2-Aminoadenosine can also act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9027-72-9 |
References: |
1. |
Lindberg, B., Klenow, H. and Hansen, K. Some properties of partially purified mammalian adenosine kinase. J. Biol. Chem. 242 (1967) 350–356. [PMID: 4290214] |
2. |
Caputto, R. The enzymatic synthesis of adenylic acid; adenosinekinase. J. Biol. Chem. 189 (1951) 801–814. [PMID: 14832298] |
3. |
Kornberg, A. and Pricer, W.E. Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside. J. Biol. Chem. 193 (1951) 481–495. [PMID: 14907737] |
|
[EC 2.7.1.20 created 1961] |
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|
EC |
2.7.1.21 |
Accepted name: |
thymidine kinase |
Reaction: |
ATP + thymidine = ADP + dTMP |
Glossary: |
dTMP = thymidine 5′-phosphate |
Other name(s): |
thymidine kinase (phosphorylating); 2′-deoxythymidine kinase; deoxythymidine kinase (phosphorylating) |
Systematic name: |
ATP:thymidine 5′-phosphotransferase |
Comments: |
Deoxyuridine can also act as acceptor, and dGTP can act as a donor. The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyses this reaction as well as those of EC 2.7.1.114 (AMP—thymidine kinase), EC 2.7.1.118 (ADP—thymidine kinase) and EC 2.7.4.9 (dTMP-kinase). |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9002-06-6 |
References: |
1. |
Falke, D., Labenz, J., Brauer, D. and Muller, W.E.G. Adenosine diphosphate: thymidine 5′-phosphotransferase, a new enzyme activity, associated with the Herpes simplex virus-induced deoxypyrimidine kinase. Biochim. Biophys. Acta 708 (1982) 99–103. [DOI] [PMID: 6293576] |
2. |
Kizer, D.E. and Holman, L. Purification and properties of thymidine kinase from regenerating rat liver. Biochim. Biophys. Acta 350 (1974) 193–200. [DOI] [PMID: 4407348] |
3. |
Okazaki, R. and Kornberg, A. Deoxythymidine kinase of Escherichia coli. I. Purification and some properties of the enzyme. J. Biol. Chem. 239 (1964) 269–274. [PMID: 14114853] |
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[EC 2.7.1.21 created 1961, deleted 1972, reinstated 1976 (EC 2.7.1.75 created 1972, incorporated 1976)] |
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EC |
2.7.1.22 |
Accepted name: |
ribosylnicotinamide kinase |
Reaction: |
ATP + 1-(β-D-ribofuranosyl)-nicotinamide = ADP + β-nicotinamide D-ribonucleotide |
Other name(s): |
ribosylnicotinamide kinase (phosphorylating); ATP:N-ribosylnicotinamide 5′-phosphotransferase |
Systematic name: |
ATP:1-(β-D-ribofuranosyl)-nicotinamide 5′-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-61-9 |
References: |
1. |
Rowen, J.W. and Kornberg, A. The phosphorolysis of nicotinamide riboside. J. Biol. Chem. 193 (1951) 497–507. [PMID: 14907738] |
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[EC 2.7.1.22 created 1961] |
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EC |
2.7.1.23 |
Accepted name: |
NAD+ kinase |
Reaction: |
ATP + NAD+ = ADP + NADP+ |
|
For diagram of NADP+ biosynthesis, click here |
Other name(s): |
DPN kinase; nicotinamide adenine dinucleotide kinase (phosphorylating); nicotinamide adenine dinucleotide kinase; NAD kinase; NADK |
Systematic name: |
ATP:NAD+ 2′-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-66-0 |
References: |
1. |
Butler, J.R. and McGuinness, E.T. Candida utilis NAD+ kinase: purification, properties and affinity gel studies. Int. J. Biochem. 14 (1982) 839–844. [PMID: 6290285] |
2. |
Chung, A.E. Nicotinamide adenine dinucleotide kinase from Azotobacter vinelandii. I. Purification and properties of the enzyme. J. Biol. Chem. 242 (1967) 1182–1186. [PMID: 4290316] |
3. |
Kornberg, A. Enzymatic synthesis of triphosphopyridine nucleotide. J. Biol. Chem. 182 (1950) 805–813. |
4. |
Wang, T.P. and Kaplan, N.O. Kinases for the synthesis of coenzyme A and triphosphopyridine nucleotide. J. Biol. Chem. 206 (1954) 311–325. [PMID: 13130551] |
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[EC 2.7.1.23 created 1961] |
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EC |
2.7.1.24 |
Accepted name: |
dephospho-CoA kinase |
Reaction: |
ATP + 3′-dephospho-CoA = ADP + CoA |
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For diagram of the late stages of CoA biosynthesis, click here |
Other name(s): |
dephosphocoenzyme A kinase (phosphorylating); 3′-dephospho-CoA kinase; dephosphocoenzyme A kinase; ATP:dephospho-CoA 3′-phosphotransferase |
Systematic name: |
ATP:3′-dephospho-CoA 3′-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-83-9 |
References: |
1. |
Abiko, Y. Pantothenic acid and coenzyme A:dephospho-CoA pyrophosphorylase and dephospho-CoA kinase as a possible bifunctional enzyme complex (ATP:pantetheine-4′-phosphate adenylyltransferase, EC 2.7.7.3 and ATP:dephospho-CoA-3′-phosphotransferase EC 2.7.1.24). Methods Enzymol. 18A (1970) 358–364. |
2. |
Hoagland, M.B. and Novelli, G.D. Biosynthesis of coenzyme A from phosphopantetheine and pantetheine from pantothenate. J. Biol. Chem. 207 (1954) 767–773. [PMID: 13163064] |
3. |
Wang, T.P. and Kaplan, N.O. Kinases for the synthesis of coenzyme A and triphosphopyridine nucleotide. J. Biol. Chem. 206 (1954) 311–325. [PMID: 13130551] |
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[EC 2.7.1.24 created 1961] |
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EC |
2.7.1.25 |
Accepted name: |
adenylyl-sulfate kinase |
Reaction: |
ATP + adenylyl sulfate = ADP + 3′-phosphoadenylyl sulfate |
Glossary: |
3′-phosphoadenylyl sulfate = PAPS |
Other name(s): |
adenylylsulfate kinase (phosphorylating); 5′-phosphoadenosine sulfate kinase; adenosine 5′-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5′-phosphosulfate-3′-phosphokinase; APS kinase |
Systematic name: |
ATP:adenylyl-sulfate 3′-phosphotransferase |
Comments: |
The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5′-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25). |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9012-38-8 |
References: |
1. |
Bandurski, R.S., Wilson, L.G., Squires, C.L. The mechanism of "active sulfate" formation. J. Am. Chem. Soc. 78 (1956) 6408–6409. |
2. |
Robbins, P.W., Lipmann, F. Isolation and identification of active sulfate. J. Biol. Chem. 229 (1957) 837–851. [PMID: 13502346] |
3. |
Venkatachalam, K.V., Akita, H., Strott, C. Molecular cloning, expression and characterization of human bifunctional 3′-phosphoadenosine-5′-phosphosulfate synthase and its functional domains. J. Biol. Chem. 273 (1998) 19311–19320. [DOI] [PMID: 9668121] |
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[EC 2.7.1.25 created 1961, modified 1999] |
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EC |
2.7.1.26 |
Accepted name: |
riboflavin kinase |
Reaction: |
ATP + riboflavin = ADP + FMN |
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For diagram of FAD biosynthesis, click here |
Other name(s): |
flavokinase; FK; RFK |
Systematic name: |
ATP:riboflavin 5′-phosphotransferase |
Comments: |
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [5]. While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase [5]. A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP [6]. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9032-82-0 |
References: |
1. |
Chassy, B.M., Arsenis, C. and McCormick, D.B. The effect of the length of the side chain of flavins on reactivity with flavokinase. J. Biol. Chem. 240 (1965) 1338–1340. [PMID: 14284745] |
2. |
Giri, K.V., Krishnaswamy, P.R. and Rao, N.A. Studies on plant flavokinase. Biochem. J. 70 (1958) 66–71. [PMID: 13584303] |
3. |
Kearney, E.B. The interaction of yeast flavokinase with riboflavin analogues. J. Biol. Chem. 194 (1952) 747–754. [PMID: 14927668] |
4. |
McCormick, D.B. and Butler, R.C. Substrate specificity of liver flavokinase. Biochim. Biophys. Acta 65 (1962) 326–332. |
5. |
Sandoval, F.J. and Roje, S. An FMN hydrolase is fused to a riboflavin kinase homolog in plants. J. Biol. Chem. 280 (2005) 38337–38345. [DOI] [PMID: 16183635] |
6. |
Solovieva, I.M., Tarasov, K.V. and Perumov, D.A. Main physicochemical features of monofunctional flavokinase from Bacillus subtilis. Biochemistry (Mosc.) 68 (2003) 177–181. [PMID: 12693963] |
7. |
Solovieva, I.M., Kreneva, R.A., Leak, D.J. and Perumov, D.A. The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon. Microbiology 145 (1999) 67–73. [DOI] [PMID: 10206712] |
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[EC 2.7.1.26 created 1961, modified 2007] |
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EC |
2.7.1.27 |
Accepted name: |
erythritol kinase (D-erythritol 4-phosphate-forming) |
Reaction: |
ATP + erythritol = ADP + D-erythritol 4-phosphate |
Other name(s): |
erythritol kinase (phosphorylating) (ambiguous) |
Systematic name: |
ATP:erythritol 4-phosphotransferase |
Comments: |
The enzyme has been characterized from the bacterium Propionibacterium acidipropionici (previously known as Propionibacterium pentosaceum). cf. EC 2.7.1.215, erythritol kinase (L-erythritol 4-phosphate-forming). |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9030-64-2 |
References: |
1. |
Shetter, J.K. Formation of D-erythritol 4-phosphate by Propionibacterium pentosaceum. J. Am. Chem. Soc. 78 (1956) 3722–3723. |
2. |
Holten, D. and Fromm, H.J. Purification and properties of erythritol kinase from Propionibacterium pentosaceum. J. Biol. Chem. 236 (1961) 2581–2584. [PMID: 13908588] |
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[EC 2.7.1.27 created 1961, modified 2016] |
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EC |
2.7.1.28 |
Accepted name: |
triokinase |
Reaction: |
ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate |
Other name(s): |
triose kinase; |
Systematic name: |
ATP:D-glyceraldehyde 3-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9030-65-3 |
References: |
1. |
Hers, H.G. and Kusaka, T. Le metabolisme du fructose-1-phosphate dans le foie. Biochim. Biophys. Acta 11 (1953) 427–437. [PMID: 13093749] |
2. |
Sillero, M.A.G., Sillero, A. and Sols, A. Enzymes involved in fructose metabolism in liver and the glyceraldehyde metabolic crossroads. Eur. J. Biochem. 10 (1969) 345–350. [DOI] [PMID: 5823111] |
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[EC 2.7.1.28 created 1961] |
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EC |
2.7.1.29 |
Accepted name: |
glycerone kinase |
Reaction: |
ATP + glycerone = ADP + glycerone phosphate |
Glossary: |
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate |
Other name(s): |
dihydroxyacetone kinase; acetol kinase; acetol kinase (phosphorylating) |
Systematic name: |
ATP:glycerone phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 57657-66-6 |
References: |
1. |
Sellinger, O.Z. and Miller, O.N. Phosphorylation of acetol by homogenates of rat liver. Fed. Proc. 16 (1957) 245–246. |
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[EC 2.7.1.29 created 1961] |
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EC |
2.7.1.30 |
Accepted name: |
glycerol kinase |
Reaction: |
ATP + glycerol = ADP + sn-glycerol 3-phosphate |
Other name(s): |
glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase |
Systematic name: |
ATP:glycerol 3-phosphotransferase |
Comments: |
Glycerone and L-glyceraldehyde can act as acceptors; UTP (and, in the case of the yeast enzyme, ITP and GTP) can act as donors. |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-66-4 |
References: |
1. |
Bergmeyer, H.-U., Holz, G., Kauder, E.M., Möllering, H. and Wieland, O. Kristallisierte Glycerokinase aus Candida mycoderma. Biochem. Z. 333 (1961) 471–480. |
2. |
Bublitz, C. and Kennedy, E.P. Synthesis of phosphatides in isolated mitochondria. III. The enzymatic phosphorylation of glycerol. J. Biol. Chem. 211 (1955) 951–961. [PMID: 13221600] |
3. |
Wieland, O. and Suyter, M. Glycerokinase: Isolierung und Eigenschaften des Enzyms. Biochem. Z. 329 (1957) 320–331. [PMID: 13522709] |
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[EC 2.7.1.30 created 1961] |
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EC |
2.7.1.31 |
Accepted name: |
glycerate 3-kinase |
Reaction: |
ATP + D-glycerate = ADP + 3-phospho-D-glycerate |
Other name(s): |
glycerate kinase (phosphorylating) (ambiguous); D-glycerate 3-kinase; D-glycerate kinase (ambiguous); glycerate-kinase (ambiguous); GK (ambiguous); D-glyceric acid kinase (ambiguous); ATP:(R)-glycerate 3-phosphotransferase |
Systematic name: |
ATP:D-glycerate 3-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-61-3 |
References: |
1. |
Doughty, C.C., Hayashi, J.A. and Guenther, H.L. Purification and properties of D-glycerate 3-kinase from Escherichia coli. J. Biol. Chem. 241 (1966) 568–572. [PMID: 5325263] |
2. |
Ichihara, A. and Greenberg, D.M. Studies on the purification and properties of D-glyceric acid kinase of liver. J. Biol. Chem. 225 (1957) 949–958. [PMID: 13416296] |
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[EC 2.7.1.31 created 1961, modified 2012] |
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EC |
2.7.1.32 |
Accepted name: |
choline kinase |
Reaction: |
ATP + choline = ADP + phosphocholine |
Other name(s): |
choline kinase (phosphorylating); choline phosphokinase; choline-ethanolamine kinase |
Systematic name: |
ATP:choline phosphotransferase |
Comments: |
Ethanolamine and its methyl and ethyl derivatives can also act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-67-9 |
References: |
1. |
Hayashi, S. and Lin, E.C.C. Purification and properties of glycerol kinase from Escherichia coli. J. Biol. Chem. 242 (1967) 1030–1035. [PMID: 5335908] |
2. |
Wittenberg, J. and Kornberg, A. Choline phosphokinase. J. Biol. Chem. 202 (1953) 431–444. [PMID: 13061469] |
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[EC 2.7.1.32 created 1961] |
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EC |
2.7.1.33 |
Accepted name: |
pantothenate kinase |
Reaction: |
ATP + (R)-pantothenate = ADP + (R)-4′-phosphopantothenate |
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For diagram of the late stages of CoA biosynthesis, click here |
Other name(s): |
pantothenate kinase (phosphorylating); pantothenic acid kinase; ATP:pantothenate 4′-phosphotransferase; D-pantothenate kinase |
Systematic name: |
ATP:(R)-pantothenate 4′-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-48-6 |
References: |
1. |
Abiko, Y., Ashida, S.-I. and Shimizu, M. Purification and properties of D-pantothenate kinase from rat liver. Biochim. Biophys. Acta 268 (1972) 364–372. [DOI] [PMID: 4337331] |
2. |
Brown, G.M. The metabolism of pantothenic acid. J. Biol. Chem. 234 (1959) 370–378. [PMID: 13630913] |
3. |
Pierpoint, W.S., Hughes, D.E., Baddiley, J. and Mathias, A.P. The phosphorylation of pantothenic acid by Lactobacillus arabinosus 17-5. Biochem. J. 61 (1955) 368–374. [PMID: 13269369] |
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[EC 2.7.1.33 created 1961] |
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EC |
2.7.1.34 |
Accepted name: |
pantetheine kinase |
Reaction: |
ATP + pantetheine = ADP + pantetheine 4′-phosphate |
Other name(s): |
pantetheine kinase (phosphorylating) |
Systematic name: |
ATP:pantetheine 4′-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9026-49-7 |
References: |
1. |
Novelli, G.D. Enzymatic synthesis and structure of CoA. Fed. Proc. 12 (1953) 675–682. [PMID: 13107738] |
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[EC 2.7.1.34 created 1961] |
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EC |
2.7.1.35 |
Accepted name: |
pyridoxal kinase |
Reaction: |
ATP + pyridoxal = ADP + pyridoxal 5′-phosphate |
Other name(s): |
pyridoxal kinase (phosphorylating); pyridoxal 5-phosphate-kinase; pyridoxal phosphokinase; pyridoxine kinase |
Systematic name: |
ATP:pyridoxal 5′-phosphotransferase |
Comments: |
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-42-0 |
References: |
1. |
McCormick, D.B., Gregory, M.E. and Snell, E.E. Pyridoxal phosphokinases. I. Assay, distribution, purification, and properties. J. Biol. Chem. 236 (1961) 2076–2084. [PMID: 13773826] |
2. |
Trufanov, A.F. and Krisanova, J.A. Biosynthesis of pyridoxal phosphate by liver sections of rat in vitro. Byull. Eksp. Biol. Med. 22(6) (1946) 40–43. |
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[EC 2.7.1.35 created 1961] |
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EC |
2.7.1.36 |
Accepted name: |
mevalonate kinase |
Reaction: |
ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate |
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For diagram of terpenoid biosynthesis, click here |
Other name(s): |
mevalonate kinase (phosphorylating); mevalonate phosphokinase; mevalonic acid kinase; mevalonic kinase; mevalonate 5-phosphotransferase ; MVA kinase; ATP:mevalonate 5-phosphotransferase |
Systematic name: |
ATP:(R)-mevalonate 5-phosphotransferase |
Comments: |
CTP, GTP and UTP can also act as donors. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-52-2 |
References: |
1. |
Hellig, H. and Popják, G. Studies on the biosynthesis of cholesterol. XIII. Phosphomevalonic kinase from liver. J. Lipid Res. 2 (1961) 235–243. |
2. |
Levy, G.B. and Popják, G. Studies on the biosynthesis of cholesterol. 10. Mevalonic kinase from liver. Biochem. J. 75 (1960) 417–428. [PMID: 14416398] |
3. |
Markley, K. and Smallman, E. Mevalonic kinase in rabbit liver. Biochim. Biophys. Acta 47 (1961) 327–335. |
4. |
Tchen, T.T. Mevalonic kinase: purification and properties. J. Biol. Chem. 233 (1958) 1100–1103. [PMID: 13598740] |
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[EC 2.7.1.36 created 1961] |
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EC
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2.7.1.37
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Transferred entry: | protein kinase. Now divided into EC 2.7.11.1 (non-specific serine/threonine protein kinase), EC 2.7.11.8 (Fas-activated serine/threonine kinase), EC 2.7.11.9 (Goodpasture-antigen-binding protein kinase), EC 2.7.11.10 (IκB kinase), EC 2.7.11.11 (cAMP-dependent protein kinase), EC 2.7.11.12 (cGMP-dependent protein kinase), EC 2.7.11.13 (protein kinase C), EC 2.7.11.21 (polo kinase), EC 2.7.11.22 (cyclin-dependent kinase), EC 2.7.11.24 (mitogen-activated protein kinase), EC 2.7.11.25 (mitogen-activated protein kinase kinase kinase), EC 2.7.11.30 (receptor protein serine/threonine kinase) and EC 2.7.12.1 (dual-specificity kinase)
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[EC 2.7.1.37 created 1961 (EC 2.7.1.70 incorporated 2004), deleted 2005] |
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EC
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2.7.1.38
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Transferred entry: | phosphorylase kinase. Now EC 2.7.11.19, phosphorylase kinase
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[EC 2.7.1.38 created 1961, deleted 2005] |
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EC |
2.7.1.39 |
Accepted name: |
homoserine kinase |
Reaction: |
ATP + L-homoserine = ADP + O-phospho-L-homoserine |
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For diagram of threonine biosynthesis, click here |
Other name(s): |
homoserine kinase (phosphorylating); HSK |
Systematic name: |
ATP:L-homoserine O-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-58-8 |
References: |
1. |
Flavin, M. and Slaughter, C. Purification and properties of threonine synthetase of Neurospora. J. Biol. Chem. 235 (1960) 1103–1108. [PMID: 13823379] |
2. |
Watanabe, Y., Konishi, S. and Shimura, K. Biosynthesis of threonine from homoserine. VI. Homoserine kinase. J. Biochem. (Tokyo) 44 (1957) 299–307. |
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[EC 2.7.1.39 created 1961] |
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EC |
2.7.1.40 |
Accepted name: |
pyruvate kinase |
Reaction: |
ATP + pyruvate = ADP + phosphoenolpyruvate |
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For diagram of the Entner-Doudoroff pathway, click here |
Other name(s): |
phosphoenolpyruvate kinase; phosphoenol transphosphorylase |
Systematic name: |
ATP:pyruvate 2-O-phosphotransferase |
Comments: |
UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2. |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-59-6 |
References: |
1. |
Boyer, P.D. Pyruvate kinase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 95–113. |
2. |
Kornberg, A. and Pricer, W.E. Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside. J. Biol. Chem. 193 (1951) 481–495. [PMID: 14907737] |
3. |
Kubowitz, F. and Ott, P. Isolierung von Gärungsfermenten aus menschlichen Muskeln. Biochem. Z. 317 (1944) 193–203. |
4. |
Strominger, J.L. Enzymatic synthesis of guanosine and cytidine triphosphates: a note on the nucleotide specificity of the pyruvate phosphokinase reaction. Biochim. Biophys. Acta 16 (1955) 616–618. [DOI] [PMID: 14389299] |
5. |
Tietz, A. and Ochoa, S. "Fluorokinase" and pyruvic kinase. Arch. Biochem. Biophys. 78 (1958) 477–493. [DOI] [PMID: 13618030] |
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[EC 2.7.1.40 created 1961] |
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EC |
2.7.1.41 |
Accepted name: |
glucose-1-phosphate phosphodismutase |
Reaction: |
2 D-glucose 1-phosphate = D-glucose + D-glucose 1,6-bisphosphate |
Systematic name: |
D-glucose-1-phosphate:D-glucose-1-phosphate 6-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9026-25-9 |
References: |
1. |
Leloir, L.F., Trucco, R.E., Cardini, C.E., Paladini, A.C. and Caputto, R. The formation of glucose diphosphate by Escherichia coli. Arch. Biochem. 24 (1949) 65–74. [PMID: 15400363] |
2. |
Sidbury, J.B., Rosenberg, L.L. and Najjar, V.A. Muscle glucose-1-phosphate transphosphorylase. J. Biol. Chem. 222 (1956) 89–96. [PMID: 13366982] |
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[EC 2.7.1.41 created 1961] |
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EC |
2.7.1.42 |
Accepted name: |
riboflavin phosphotransferase |
Reaction: |
α-D-glucose 1-phosphate + riboflavin = D-glucose + FMN |
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For diagram of FAD biosynthesis, click here |
Other name(s): |
riboflavine phosphotransferase; glucose-1-phosphate phosphotransferase; G-1-P phosphotransferase; D-glucose-1-phosphate:riboflavin 5′-phosphotransferase |
Systematic name: |
α-D-glucose-1-phosphate:riboflavin 5′-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-26-0 |
References: |
1. |
Katagiri, H., Yamada, H. and Imai, K. The transphosphorylation reactions catalyzed by glucose 1-phosphate phosphotransferases of Escherichia coli. I. Enzymic phosphorylation of riboflavine. J. Biochem. (Tokyo) 46 (1959) 1119–1126. |
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[EC 2.7.1.42 created 1961] |
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EC |
2.7.1.43 |
Accepted name: |
glucuronokinase |
Reaction: |
ATP + D-glucuronate = ADP + 1-phospho-α-D-glucuronate |
Other name(s): |
glucuronokinase (phosphorylating); glucurono-glucuronokinase |
Systematic name: |
ATP:D-glucuronate 1-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-62-4 |
References: |
1. |
Neufeld, E.F., Feingold, D.S. and Hassid, W.Z. Enzymic phosphorylation of D-glucuronic acid by extracts from seedlings of Phaseolus aureus. Arch. Biochem. Biophys. 83 (1959) 96–100. [DOI] [PMID: 13661996] |
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[EC 2.7.1.43 created 1965] |
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EC |
2.7.1.44 |
Accepted name: |
galacturonokinase |
Reaction: |
ATP + D-galacturonate = ADP + 1-phospho-α-D-galacturonate |
Other name(s): |
galacturonokinase (phosphorylating) D-galacturonic acid kinase |
Systematic name: |
ATP:D-galacturonate 1-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-63-5 |
References: |
1. |
Neufeld, E.F., Feingold, D.S., Ilves, S.M., Kessler, G. and Hassid, W.Z. Phosphorylation of D-galacturonic acid by extracts from germinating seeds of Phaseolus aureus. J. Biol. Chem. 236 (1961) 3102–3105. [PMID: 14479161] |
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[EC 2.7.1.44 created 1965] |
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EC |
2.7.1.45 |
Accepted name: |
2-dehydro-3-deoxygluconokinase |
Reaction: |
ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate |
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For diagram of the Entner-Doudoroff pathway, click here |
Other name(s): |
2-keto-3-deoxygluconokinase; 2-keto-3-deoxy-D-gluconic acid kinase; 2-keto-3-deoxygluconokinase (phosphorylating); 2-keto-3-deoxygluconate kinase; ketodeoxygluconokinase |
Systematic name: |
ATP:2-dehydro-3-deoxy-D-gluconate 6-phosphotransferase |
Comments: |
The enzyme shows no activity with 2-dehydro-3-deoxy-D-galactonate [1]. cf. EC 2.7.1.178, 2-dehydro-3-deoxyglucono/2-dehydro-3-deoxygalactonokinase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-54-4 |
References: |
1. |
Cynkin, M.A. and Ashwell, G. Uronic acid metabolism in bacteria. IV. Purification and properties of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli. J. Biol. Chem. 235 (1960) 1576–1579. [PMID: 13813474] |
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[EC 2.7.1.45 created 1965, modified 1976] |
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EC |
2.7.1.46 |
Accepted name: |
L-arabinokinase |
Reaction: |
ATP + L-arabinose = ADP + β-L-arabinose 1-phosphate |
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For diagram of UDP-L-arabinose, UDP-galacturonate and UDP-xylose biosynthesis, click here |
Other name(s): |
L-arabinokinase (phosphorylating) |
Systematic name: |
ATP:L-arabinose 1-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 37277-99-9 |
References: |
1. |
Neufeld, E.F., Feingold, D.S. and Hassid, W.Z. Phosphorylation of D-galactose and L-arabinose by extracts from Phaseolus aureus seedlings. J. Biol. Chem. 235 (1960) 906–909. [PMID: 14426659] |
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[EC 2.7.1.46 created 1965] |
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EC |
2.7.1.47 |
Accepted name: |
D-ribulokinase |
Reaction: |
ATP + D-ribulose = ADP + D-ribulose 5-phosphate |
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For diagram of D-Arabinose catabolism, click here |
Other name(s): |
D-ribulokinase (phosphorylating) |
Systematic name: |
ATP:D-ribulose 5-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-40-8 |
References: |
1. |
Fromm, H.J. D-Ribulokinase from Aerobacter aerogenes. J. Biol. Chem. 234 (1959) 3097–3101. [PMID: 13825363] |
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[EC 2.7.1.47 created 1965] |
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EC |
2.7.1.48 |
Accepted name: |
uridine/cytidine kinase |
Reaction: |
(1) ATP + uridine = ADP + UMP (2) ATP + cytidine = ADP + CMP |
Other name(s): |
UCK (gene name); URK1 (gene name); pyrimidine ribonucleoside kinase; uridine-cytidine kinase; uridine kinase (phosphorylating); uridine phosphokinase; ATP:uridine 5′-phosphotransferase; uridine kinase |
Systematic name: |
ATP:uridine/cytidine 5′-phosphotransferase |
Comments: |
The enzyme, found in prokaryotes and eukaryotes, phosphorylates both uridine and cytidine to their monophosphate forms. The enzyme from Escherichia coli prefers GTP to ATP. The human enzyme also catalyses the phosphorylation of several cytotoxic ribonucleoside analogs. cf. EC 2.7.1.213, cytidine kinase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-39-5 |
References: |
1. |
Sköld, O. Uridine kinase from Erlich ascites tumor: purification and properties. J. Biol. Chem. 235 (1960) 3273–3279. |
2. |
Orengo, A. Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor. J. Biol. Chem. 244 (1969) 2204–2209. [PMID: 5782006] |
3. |
Valentin-Hansen, P. Uridine-cytidine kinase from Escherichia coli. Methods Enzymol. 51 (1978) 308–314. [PMID: 211379] |
4. |
Kern, L. The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase. Nucleic Acids Res. 18:5279 (1990). [PMID: 2169608] |
5. |
Van Rompay, A.R., Norda, A., Linden, K., Johansson, M. and Karlsson, A. Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol. Pharmacol. 59 (2001) 1181–1186. [PMID: 11306702] |
6. |
Ohler, L., Niopek-Witz, S., Mainguet, S.E. and Mohlmann, T. Pyrimidine salvage: physiological functions and interaction with chloroplast biogenesis. Plant Physiol. 180 (2019) 1816–1828. [PMID: 31101721] |
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[EC 2.7.1.48 created 1965, modified 2020] |
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EC |
2.7.1.49 |
Accepted name: |
hydroxymethylpyrimidine kinase |
Reaction: |
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine |
Other name(s): |
hydroxymethylpyrimidine kinase (phosphorylating) |
Systematic name: |
ATP:4-amino-5-hydroxymethyl-2-methylpyrimidine 5-phosphotransferase |
Comments: |
CTP, UTP and GTP can act as donors. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-55-5 |
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. |
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[EC 2.7.1.49 created 1965] |
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EC |
2.7.1.50 |
Accepted name: |
hydroxyethylthiazole kinase |
Reaction: |
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole |
Other name(s): |
hydroxyethylthiazole kinase (phosphorylating); 4-methyl-5-(β-hydroxyethyl)thiazole kinase |
Systematic name: |
ATP:4-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-56-6 |
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. |
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[EC 2.7.1.50 created 1965] |
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