The Enzyme Database

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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, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, 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]
 
 
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, 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]
 
 
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, 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]
 
 
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, 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]
[EC 2.7.1.4 created 1961]
 
 
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, 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]
[EC 2.7.1.5 created 1961]
 
 
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, 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]
 
 
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, 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]
 
 
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 has been studied in the bacterium Vibrio cholerae, where it participates in a chitin degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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]
[EC 2.7.1.8 created 1961, modified 2014]
 
 
EC 2.7.1.9      
Deleted entry:  acetylaminodeoxyglucose kinase
[EC 2.7.1.9 created 1961, deleted 1965]
 
 
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]
 
 
EC 2.7.1.11     
Accepted name: 6-phosphofructokinase
Reaction: ATP + D-fructose 6-phosphate = ADP + D-fructose 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:D-fructose-6-phosphate 1-phosphotransferase
Comments: 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, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-80-3
References:
1.  Axelrod, B., Saltman, P., Bandurski, R.S. and Baker, R.S. Hexokinase in higher plants. J. Biol. Chem. 197 (1952) 89–96. [PMID: 12981037]
2.  Ling, K.H., Pastkau, V., Marcus, F. and Lardy, H.A. Phosphofructokinase. I. Skeletal muscle. Methods Enzymol. 9 (1966) 425–429.
3.  Mansour, T.E. Phosphofructokinase. II. Heart muscle. Methods Enzymol. 9 (1966) 430–436.
4.  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]
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.  Racker, E. Spectrophotometric measurement of hexokinase and phosphohexokinase activity. J. Biol. Chem. 167 (1947) 843–854. [PMID: 20287918]
7.  Sols, A. and Salas, M.L. Phosphofructokinase. III. Yeast. Methods Enzymol. 9 (1966) 436–442.
8.  Uyeda, K. and Kurooka, S. Crystallization and properties of phosphofructokinase from Clostridium pasteurianum. J. Biol. Chem. 245 (1970) 3315–3324. [PMID: 4248230]
[EC 2.7.1.11 created 1961]
 
 
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, 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]
[EC 2.7.1.12 created 1961]
 
 
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, 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]
[EC 2.7.1.13 created 1961]
 
 
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, 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]
 
 
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, 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]
 
 
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, KEGG, MetaCyc, 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]
[EC 2.7.1.16 created 1961]
 
 
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, 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.
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]
 
 
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]
 
 
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, 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]
 
 
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, 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]
 
 
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, 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]
[EC 2.7.1.21 created 1961, deleted 1972, reinstated 1976 (EC 2.7.1.75 created 1972, incorporated 1976)]
 
 
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, KEGG, MetaCyc, 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]
[EC 2.7.1.22 created 1961]
 
 
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, 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]
[EC 2.7.1.23 created 1961]
 
 
EC 2.7.1.24     
Accepted name: dephospho-CoA kinase
Reaction: ATP + 3′-dephospho-CoA = ADP + CoA
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, 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]
[EC 2.7.1.24 created 1961]
 
 
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, 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]
[EC 2.7.1.25 created 1961, modified 1999]
 
 
EC 2.7.1.26     
Accepted name: riboflavin kinase
Reaction: ATP + riboflavin = ADP + FMN
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, 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]
[EC 2.7.1.26 created 1961, modified 2007]
 
 
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, KEGG, MetaCyc, 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]
[EC 2.7.1.27 created 1961, modified 2016]
 
 
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, 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]
[EC 2.7.1.28 created 1961]
 
 
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, 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.
[EC 2.7.1.29 created 1961]
 
 
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, 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]
[EC 2.7.1.30 created 1961]
 
 
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, 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]
[EC 2.7.1.31 created 1961, modified 2012]
 
 
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, 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]
[EC 2.7.1.32 created 1961]
 
 
EC 2.7.1.33     
Accepted name: pantothenate kinase
Reaction: ATP + (R)-pantothenate = ADP + (R)-4′-phosphopantothenate
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, 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]
[EC 2.7.1.33 created 1961]
 
 
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, 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]
[EC 2.7.1.34 created 1961]
 
 
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, 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.
[EC 2.7.1.35 created 1961]
 
 
EC 2.7.1.36     
Accepted name: mevalonate kinase
Reaction: ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
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, 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]
[EC 2.7.1.36 created 1961]
 
 
EC 2.7.1.37      
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)
[EC 2.7.1.37 created 1961 (EC 2.7.1.70 incorporated 2004), deleted 2005]
 
 
EC 2.7.1.38      
Transferred entry: phosphorylase kinase. Now EC 2.7.11.19, phosphorylase kinase
[EC 2.7.1.38 created 1961, deleted 2005]
 
 
EC 2.7.1.39     
Accepted name: homoserine kinase
Reaction: ATP + L-homoserine = ADP + O-phospho-L-homoserine
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, 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.
[EC 2.7.1.39 created 1961]
 
 
EC 2.7.1.40     
Accepted name: pyruvate kinase
Reaction: ATP + pyruvate = ADP + phosphoenolpyruvate
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, 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. (Eds), 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]
[EC 2.7.1.40 created 1961]
 
 
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, 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]
[EC 2.7.1.41 created 1961]
 
 
EC 2.7.1.42     
Accepted name: riboflavin phosphotransferase
Reaction: α-D-glucose 1-phosphate + riboflavin = D-glucose + FMN
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.
[EC 2.7.1.42 created 1961]
 
 
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]
[EC 2.7.1.43 created 1965]
 
 
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]
[EC 2.7.1.44 created 1965]
 
 
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
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, KEGG, MetaCyc, 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]
[EC 2.7.1.45 created 1965, modified 1976]
 
 
EC 2.7.1.46     
Accepted name: L-arabinokinase
Reaction: ATP + L-arabinose = ADP + β-L-arabinose 1-phosphate
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, 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]
[EC 2.7.1.46 created 1965]
 
 
EC 2.7.1.47     
Accepted name: D-ribulokinase
Reaction: ATP + D-ribulose = ADP + D-ribulose 5-phosphate
Other name(s): D-ribulokinase (phosphorylating)
Systematic name: ATP:D-ribulose 5-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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]
[EC 2.7.1.47 created 1965]
 
 
EC 2.7.1.48     
Accepted name: uridine kinase
Reaction: ATP + uridine = ADP + UMP
Other name(s): pyrimidine ribonucleoside kinase; uridine-cytidine kinase; uridine kinase (phosphorylating); uridine phosphokinase
Systematic name: ATP:uridine 5′-phosphotransferase
Comments: Cytidine can act as acceptor; GTP and ITP can act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-39-5
References:
1.  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]
2.  Sköld, O. Uridine kinase from Erlich ascites tumor: purification and properties. J. Biol. Chem. 235 (1960) 3273–3279.
[EC 2.7.1.48 created 1965]
 
 
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, KEGG, MetaCyc, 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.
[EC 2.7.1.49 created 1965]
 
 
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, 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.
[EC 2.7.1.50 created 1965]
 
 


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