Continued from EC 2.7.1.151 to EC 2.7.1.239
EC 2.7.2 Phosphotransferases with a carboxy group as acceptor
EC 2.7.3 Phosphotransferases with a nitrogenous group as acceptor
Accepted name: acetate kinase
Reaction: ATP + acetate = ADP + acetyl phosphate
Other name(s): acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating)
Systematic name: ATP:acetate phosphotransferase
Comments: Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate [4], others have found that the enzyme can also use propanoate as a substrate, but more slowly [7]. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate [9].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-42-3
References:
1. Romain, Y., Demassieux, S. and Carriere, S. Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines. Biochem. Biophys. Res. Commun. 106 (1982) 999-1005. [PMID: 6956338]
2. Romano, A.H. and Nickerson, W.J. Cystine reductase of pea seeds and yeasts. J. Biol. Chem. 208 (1954) 409-416. [PMID: 13174550]
3. Stern, J.R. and Ochoa, S. Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes. J. Biol. Chem. 191 (1951) 161-172. [PMID: 14850456]
4. Fox, D.K. and Roseman, S. Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli. J. Biol. Chem. 261 (1986) 13487-13497. [PMID: 3020034]
5. Knorr, R., Ehrmann, M.A. and Vogel, R.F. Cloning, expression, and characterization of acetate kinase from Lactobacillus sanfranciscensis. Microbiol. Res. 156 (2001) 267-277. [PMID: 11716215]
6. Buss, K.A., Cooper, D.R., Ingram-Smith, C., Ferry, J.G., Sanders, D.A. and Hasson, M.S. Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. J. Bacteriol. 183 (2001) 680-686. [PMID: 11133963]
7. Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase. J. Bacteriol. 187 (2005) 2386-2394. [PMID: 15774882]
8. Gorrell, A., Lawrence, S.H. and Ferry, J.G. Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila. J. Biol. Chem. 280 (2005) 10731-10742. [PMID: 15647264]
9. Heßlinger, C., Fairhurst, S.A. and Sawers, G. Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol. Microbiol. 27 (1998) 477-492. [PMID: 9484901]
Accepted name: carbamate kinase
Reaction: ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O (overall reaction)
(1a) ATP + carbamate = ADP + carbamoyl phosphate
(1b) NH3 + hydrogencarbonate = carbamate + H2O (spontaneous)
For diagram of reaction click here
Other name(s): CKase; carbamoyl phosphokinase; carbamyl phosphokinase
Systematic name: ATP:carbamate phosphotransferase
Comments: The enzyme catalyses the reversible conversion of carbamoyl phosphate and ADP to ATP and carbamate, which hydrolyses to ammonia and hydrogencarbonate. The physiological role of the enzyme is to generate ATP.
Links to other databases: BRENDA, EXPASY, ExplorEnz, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-69-1
References:
1. Jones, M.E., Spector, L. and Lipmann, F. Carbamyl phosphate, the carbamyl donor in enzymatic citrulline synthesis. J. Am. Chem. Soc. 77 (1955) 819-820.
2. Davis, R.H. Carbamyl phosphate synthesis in Neurospora crassa. I. Preliminary characterization of arginine-specific carbamyl phosphokinase. Biochim. Biophys. Acta 107 (1965) 44-53. [PMID: 5857367]
3. Glasziou, K.T. The metabolism of arginine in Serratia marcescens. II. Carbamyladenosine diphosphate phosphoferase. Aust. J. Biol. Sci. 9 (1956) 253-262.
4. Bishop, S.H. and Grisolia, S. Crystalline carbamate kinase. Biochim. Biophys. Acta 118 (1966) 211-215. [PMID: 4959296]
5. Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532-9541. [PMID: 6895223]
Accepted name: phosphoglycerate kinase
Reaction: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
For diagram of reaction click here, another presentation click here.
Other names: PGK; 3-PGK; ATP-3-phospho-D-glycerate-1-phosphotransferase; ATP:D-3-phosphoglycerate 1-phosphotransferase; 3-phosphoglycerate kinase; 3-phosphoglycerate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid phosphokinase; 3-phosphoglyceric kinase; glycerate 3-phosphate kinase; glycerophosphate kinase; phosphoglyceric acid kinase; phosphoglyceric kinase; phosphoglycerokinase
Systematic name: ATP:3-phospho-D-glycerate 1-phosphotransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-83-6
References:
1. Axelrod, B. and Bandurski, R.S. Phosphoglyceroyl kinase in higher plants. J. Biol. Chem. 204 (1953) 939-948.
2. Bücher, T. Über ein phosphatübertragendes Gärungsferment. Biochim. Biophys. Acta 1 (1947) 292-314.
3. Hashimoto, T. and Yoshikawa, H. Crystalline phosphoglycerate kinase from human erythrocytes. Biochim. Biophys. Acta 65 (1962) 355-357.
4. Rao, D.R. and Oespar, P. Purification and properties of muscle phosphoglycerate kinase. Biochem. J. 81 (1961) 405-411.
Accepted name: aspartate kinase
Reaction: ATP + L-aspartate = ADP + 4-phospho-L-aspartate
For diagram click here.
Other name(s): aspartokinase; AK; β-aspartokinase; aspartic kinase
Systematic name: ATP:L-aspartate 4-phosphotransferase
Comments: The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase. This is also the case for two of the four isoenzymes in Arabidopsis thaliana. The equilibrium constant strongly favours the reaction from right to left, i.e. the non-physiological direction of reaction.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9012-50-4
References:
1. Black, S. Conversion of aspartic acid to homoserine. Methods Enzymol. 5 (1962) 820-827.
2. Paulus, H. and Gray, E. Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies. J. Biol. Chem. 242 (1967) 4980-4986. [PMID: 6058940]
3. Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex. Biochemistry 11 (1972) 677-687. [PMID: 4551091]
4. Véron, M., Falcoz-Kelly, F. and Cohen, G.N. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. Eur. J. Biochem. 28 (1972) 520-527. [PMID: 4562990]
[EC 2.7.2.5 Transferred entry: now EC 6.3.4.16 carbamoyl-phosphate synthase (ammonia) (EC 2.7.2.5 created 1965, deleted 1978)]
Accepted name: formate kinase
Reaction: ATP + formate = ADP + formyl phosphate
Systematic name: ATP:formate phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-65-7
References:
1. Sly, W.S. and Stadtman, E.R. Formate metabolism. II. Enzymatic synthesis of formyl phosphate and formyl coenzyme A in Clostridium cylindrosporum. J. Biol. Chem. 238 (1963) 2639-2647.
Accepted name: butyrate kinase
Reaction: ATP + butanoate = ADP + butanoyl phosphate
Systematic name: ATP:butanoate 1-phosphotransferase
Comments: The enzyme from Clostridium sp. also acts, more slowly, on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14 sedoheptulokinase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-14-1
References:
1. Hartmanis, M.G.N. Butyrate kinase from Clostridium acetobutylicum. J. Biol. Chem. 262 (1987) 617-621. [PMID: 3027059]
2. Twarog, R. and Wolfe, R.S. Enzymatic phosphorylation of butyrate. J. Biol. Chem. 237 (1962) 2474-2477.
Accepted name: acetylglutamate kinase
Reaction: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
For diagram click here.
Other names: N-acetylglutamate 5-phosphotransferase; acetylglutamate phosphokinase; N-acetylglutamate phosphokinase; N-acetylglutamate kinase; N-acetylglutamic 5-phosphotransferase
Systematic name: ATP:N-acetyl-L-glutamate 5-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-58-1
References:
1. Baich, A. and Vogel, H.J. N-Acetyl-γ-glutamokinase and N-acetylglutamic γ-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli. Biochem. Biophys. Res. Commun. 7 (1962) 491-496.
2. Faragó, A. and Dénes, G. Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. II. Purification and properties of N-acetylglutamate 5-phosphotransferase, the allosteric enzyme of the pathway. Biochim. Biophys. Acta 136 (1967) 6-18. [PMID: 6040410]
3. Vogel, H.J. and McLellan, W.L. N-Acetyl-γ-glutamokinase (Escherichia coli). Methods Enzymol. 17A (1970) 251-255.
[EC 2.7.2.9 Transferred entry: now EC 6.3.5.5 carbamoyl-phosphate synthase (glutamine-hydrolysing) (EC 2.7.2.9 created 1972, deleted 1978)]
Accepted name: phosphoglycerate kinase (GTP)
Reaction: GTP + 3-phospho-D-glycerate = GDP + 3-phospho-D-glyceroyl phosphate
Systematic name: GTP:3-phospho-D-glycerate 1-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-34-7
References:
1. Reeves, R.E. and South, D.J. Phosphoglycerate kinase (GTP). An enzyme from Entamoeba histolytica selective for guanine nucleotides. Biochem. Biophys. Res. Commun. 58 (1974) 1053-1057. [PMID: 4365563]
Accepted name: glutamate 5-kinase
Reaction: ATP + L-glutamate = ADP + L-glutamate 5-phosphate
For diagram click here.
Other names: ATP-L-glutamate 5-phosphotransferase; ATP:γ-L-glutamate phosphotransferase; γ-glutamate kinase; γ-glutamyl kinase; glutamate kinase
Systematic name: ATP:L-glutamate 5-phosphotransferase
Comments: In the absence of downstream enzymes, the product rapidly cyclizes to 5-oxo-L-proline and phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 54596-30-4
References:
1. Baich, A. Proline synthesis in Escherichia coli. A proline-inhibitable glutamic acid kinase. Biochim. Biophys. Acta 192 (1969) 462-467. [PMID: 4904678]
Accepted name: acetate kinase (diphosphate)
Reaction: diphosphate + acetate = phosphate + acetyl phosphate
Other names: pyrophosphate-acetate phosphotransferase
Systematic name: diphosphate:acetate phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 57657-58-6
References:
1. Reeves, R.E. and Guthrie, J.D. Acetate kinase (pyrophosphate). A fourth pyrophosphate-dependent kinase from Entamoeba histolytica. Biochem. Biophys. Res. Commun. 66 (1975) 1389-1395. [PMID: 172079]
[EC 2.7.2.13 Deleted entry: , now known to be due to the activities of EC 6.1.1.17, glutamate---tRNA ligase, EC 1.2.1.70, glutamyl-tRNA reductase and EC 5.4.3.8, glutamate-1-semialdehyde 2,1-aminomutase (EC 2.7.2.13 created 1984, deleted 2020)]
Accepted name: branched-chain-fatty-acid kinase
Reaction: ATP + 2-methylpropanoate = ADP + 2-methylpropanoyl phosphate
Other name(s): isobutyrate kinase
Systematic name: ATP:branched-chain-fatty-acid 1-phosphotransferase
Comments: 3-Methylbutanoate, 2-methylbutanoate, pentanoate, butanoate and propanoate can also act as acceptors (cf. EC 2.7.2.7 butyrate kinase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 84177-54-8
References:
1. Harwood, C.S. and Canale-Parola, E. Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a spirochete. J. Bacteriol. 152 (1982) 246-254. [PMID: 6288660]
Accepted name: propionate kinase
Reaction: ATP + propanoate = ADP + propanoyl phosphate
Other name(s): PduW; TdcD; propionate/acetate kinase
Systematic name: ATP:propanoate phosphotransferase
Comments: Requires Mg2+. Acetate can also act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [1]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 39369-28-3
References:
1. Heßlinger, C., Fairhurst, S.A. and Sawers, G. Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol. Microbiol. 27 (1998) 477-492. [PMID: 9484901]
2. Palacios, S., Starai, V.J. and Escalante-Semerena, J.C. Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol. J. Bacteriol. 185 (2003) 2802-2810. [PMID: 12700259]
3. Wei, Y. and Miller, C.G. Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium. J. Bacteriol. 181 (1999) 6092-6097. [PMID: 10498722]
4. Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase. J. Bacteriol. 187 (2005) 2386-2394. [PMID: 15774882]
5. Simanshu, D.K. and Murthy M.R.N. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium. Acta Crystallogr. F Struct. Biol. Cryst. Commun. 61 (2005) 52-55.
6. Simanshu, D.K., Savithri, H.S. and Murthy M.R.N. Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: Comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily. J. Mol. Biol. 2005, in press.
Accepted name: 2-phosphoglycerate kinase
Reaction: ATP + 2-phospho-D-glycerate = ADP + 2,3-diphospho-D-glycerate
Other name(s): pgk2 (gene name)
Systematic name: ATP:2-phosphoglycerate 3-phosphotransferase
Comments: The enzyme, found in a number of methanogenic archaeal genera, is involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant. Activity is stimulated by potassium ions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lehmacher, A., Vogt, A.B. and Hensel, R. Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and cyclic 2,3-diphosphoglycerate synthetase from Methanothermus fervidus. FEBS Lett. 272 (1990) 94-98. [PMID: 2226838]
2. Lehmacher, A. and Hensel, R. Cloning, sequencing and expression of the gene encoding 2-phosphoglycerate kinase from Methanothermus fervidus. Mol. Gen. Genet. 242 (1994) 163-168. [PMID: 8159166]
Accepted name: [amino group carrier protein]-L-2-aminoadipate 6-kinase
Reaction: ATP + an [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine
Other name(s): lysZ (gene name)
Systematic name: [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine 5-O-kinase
Comments: The enzyme participates in an L-lysine biosynthetric pathway in certain species of bacteria and archaea.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nishida, H., Nishiyama, M., Kobashi, N., Kosuge, T., Hoshino, T. and Yamane, H. A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. Genome Res. 9 (1999) 1175-1183. [PMID: 10613839]
2. Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673-679. [PMID: 19620981]
3. Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277-283. [PMID: 23434852]
Accepted name: fatty acid kinase
Reaction: ATP + a fatty acid = ADP + a fatty acyl phosphate (overall reaction)
(1a) ATP + a fatty acid-[fatty acid-binding protein] = ADP + a fatty acyl phosphate-[fatty acid-binding protein]
(1b) a fatty acyl phosphate-[fatty acid-binding protein] + a fatty acid = a fatty acyl phosphate + a fatty acid-[fatty acid-binding protein]
Other name(s): fakAB (gene names)
Systematic name: ATP:fatty acid 1-phosphotransferase
Comments: The enzyme is a dimeric complex consisting of an ATP-binding protein (FakA) and a fatty acid-binding protein (FakB). The first step in the reaction is the binding of FakB (with a bound fatty acid) to FakA. The fatty acid bound to FakB is then phosphorylated by FakA, and the fatty acyl phosphate-bound FakB is released from the complex. In the presence of an exchangeable fatty acid pool in the cell membrane, the fatty acy phosphate bound to FakB exchanges with a fatty acid to regenerate the substrate for FakA. The system is widespread in Gram-positive bacteria, with most strains possessing a single FakA protein along with multiple FakB subunits that differ in their specificity towards fatty acid substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Parsons, J.B., Frank, M.W., Jackson, P., Subramanian, C. and Rock, C.O. Incorporation of extracellular fatty acids by a fatty acid kinase-dependent pathway in Staphylococcus aureus. Mol. Microbiol. 92 (2014) 234-245. [PMID: 24673884]
2. Parsons, J.B., Broussard, T.C., Bose, J.L., Rosch, J.W., Jackson, P., Subramanian, C. and Rock, C.O. Identification of a two-component fatty acid kinase responsible for host fatty acid incorporation by Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 111 (2014) 10532-10537. [PMID: 25002480]
3. Broussard, T.C., Miller, D.J., Jackson, P., Nourse, A., White, S.W. and Rock, C.O. Biochemical roles for conserved residues in the bacterial fatty acid-binding protein family. J. Biol. Chem. 291 (2016) 6292-6303. [PMID: 26774272]
Accepted name: [amino-group carrier protein]-L-glutamate 6-kinase
Reaction: ATP + an [amino-group carrier protein]-C-terminal-γ-(L-glutamyl)-L-glutamate = ADP + an [amino-group carrier protein]-C-terminal-γ-(5-phospho-L-glutamyl)-L-glutamate
Other name(s): lysZ (gene name)
Systematic name: [amino-group carrier protein]-C-terminal-γ-(L-glutamyl)-L-glutamine 5-O-kinase
Comments: The enzyme participates in an L-arginine biosynthetic pathway in certain species of archaea. In some organisms the enzyme also catalyses the activity of EC 2.7.2.17, [amino-group carrier protein]-L-2-aminoadipate 6-kinase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277-283. [PMID: 23434852]
2. Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630-21643. [PMID: 27566549]
EC 2.7.3.13 glutamine kinase
Accepted name: guanidinoacetate kinase
Reaction: ATP + guanidinoacetate = ADP + phosphoguanidinoacetate
Other names: glycocyamine kinase
Systematic name: ATP:guanidinoacetate N-phosphotransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-60-2
References:
1. Hobson, G.E. and Rees, K.R. The annelid phosphokinases. Biochem. J. 65 (1957) 305-307.
2. Pradel, L.-A., Kassab, R., Conlay, C. and Thoai, N.V. Properties and amino acid composition of purified ATP: guanidinoacetate phosphotransferase. Biochim. Biophys. Acta 154 (1968) 305-314. (French). [PMID: 5637051]
3. Pradel, L.-A., Kassab, R. and Thoai, N.V. Sur l'acide adenosine-triphosphorique:guanidoacétate phosphotransferase. Biochim. Biophys. Acta 81 (1964) 86-95.
4. Thoai, N.V. Sur la taurocyamine et la glycocyamine phosphokinase. Bull. Soc. Chim. Biol. 39 (1957) 197-208.
Accepted name: creatine kinase
Reaction: ATP + creatine = ADP + phosphocreatine
For diagram of reaction click here.
Other names: ATP:creatine phosphotransferase; CK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK
Systematic name: ATP:creatine N-phosphotransferase
Comments: N-Ethylglycocyamine can also act as acceptor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-15-4
References:
1. Ennor, A.H., Rosenberg, H. and Armstrong, M.D. Specificity of creatine phosphokinase. Nature 175 (1955) 120 only.
2. Keutel, H.J., Jacobs, H.K., Okabe, K., Yue, R.H. and Kuby, S.A. Studies on adenosine triphosphate transphosphorylases. VII. Isolation of the crystalline adenosine triphosphate-creatine transphosphorylase from calf brain. Biochemistry 7 (1968) 4283-4290. [PMID: 5750168]
3. Kuby, S.A., Noda, L. and Lardy, H.A. Adenosine triphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J. Biol. Chem. 209 (1954) 191-201.
4. Kuby, S.A. and Noltmann, E.A. ATP-creatine transphosphorylase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp. 515-603.
Accepted name: arginine kinase
Reaction: ATP + L-arginine = ADP + Nω-phospho-L-arginine
Other names: arginine phosphokinase; adenosine 5'-triphosphate: L-arginine phosphotransferase; adenosine 5'-triphosphate-arginine phosphotransferase
Systematic name: ATP:L-arginine Nω-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-70-4
References:
1. Elödi, P. and Szörényi, E.T. Properties of crystalline arginine phosphoferase isolated from crustacean muscle. Acta Physiol. Acad. Sci. (Hung.) 9 (1956) 367-379.
2. Morrison, J.F., Griffiths, D.E. and Ennor, A.H. The purification and properties of arginine phosphokinase. Biochem. J. 65 (1957) 143-153.
3. Szörényi, E.T., Dvornikova, P.D. and Degtyar, P.G. [Isolation in the crystalline state and some properties of adenosinetriphosphate-arginine transphosphorylase.] Dokl. Akad. Nauk SSSR. 67 (1949) 341-344. (in Russian)
4. Virden, R., Watts, D.C. and Baldwin, E. Adenosine 5'-triphosphate-arginine phosphotransferase from lobster muscle: purification and properties. Biochem. J. 94 (1965) 536-544.
Accepted name: taurocyamine kinase
Reaction: ATP + taurocyamine = ADP + N-phosphotaurocyamine
Other names: taurocyamine phosphotransferase; ATP:taurocyamine phosphotransferase
Systematic name: ATP:taurocyamine N-phosphotransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-72-6
References:
1. Hobson, G.E. and Rees, K.R. The annelid phosphokinase. Biochem. J. 65 (1957) 305-307.
2. Kassab, R., Pradel, L.A. and Thoai, N.V. ATP:taurocyamine and ATP:lombricine phosphotransferases. Purification and study of SH groups. Biochim. Biophys. Acta 99 (1965) 397-405. (French). [PMID: 5840960]
3. Thoai, N.V. Sur la taurocyamine et la glycocyamine phosphokinase. Bull. Soc. Chim. Biol. 39 (1957) 197-208.
4. Thoai, N.V., Robin, Y. and Pradel, L.-A. Hypotaurocyamine phosphokinase comparison avec la taurocyamine phosphokinase. Biochim. Biophys. Acta 73 (1963) 437-444.
Accepted name: lombricine kinase
Reaction: ATP + lombricine = ADP + N-phospholombricine
Systematic name: ATP:lombricine N-phosphotransferase
Comments: Also acts on methylated lombricines such as thalassemine; the specificity varies with the source species.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-53-3
References:
1. Gaffney, T.J., Rosenberg, H. and Ennor, A.H. The purification and properties of adenosine triphosphate-lombricine phosphotransferase. Biochem. J. 90 (1964) 170-176. [PMID: 5832288]
2. Kassab, R., Pradel, L.A. and Thoai, N.V. ATP:taurocyamine and ATP:lombricine phosphotransferases. Purification and study of SH groups. Biochim. Biophys. Acta 99 (1965) 397-405. [PMID: 5840960]
3. Pant, R. Isolation of lombricine and its enzymatic phosphorylation. Biochem. J. 73 (1959) 30-33.
4. Thoai, N.V., Robin, Y. and Guillou, Y. A new phosphagen, N'-phosphorylguanidinoethylphospho-O-(α-N,N-dimethyl)serine (phosphothalassemine). Biochemistry 11 (1972) 3890-3895. [PMID: 5079888]
Accepted name: hypotaurocyamine kinase
Reaction: ATP + hypotaurocyamine = ADP + Nω-phosphohypotaurocyamine
Systematic name: ATP:hypotaurocyamine N-phosphotransferase
Comments: Also acts, more slowly, on taurocyamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-57-7
References:
1. Thoai, N.V., Robin, Y. and Pradel, L.-A. Hypotaurocyamine phosphokinase comparison avec la taurocyamine phosphokinase. Biochim. Biophys. Acta 73 (1963) 437-444.
Accepted name: opheline kinase
Reaction: ATP + guanidinoethyl methyl phosphate = ADP + N'-phosphoguanidinoethyl methylphosphate
Systematic name: ATP:guanidinoethyl-methyl-phosphate phosphotransferase
Comments: Has a little activity on taurocyamine, lombricine and phosphotaurocyamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-15-2
References:
1. Thoai, N.V., di Jeso, F., Robin, Y. and der Terrossian, E. Sur la nouvelle acide adenosine 5'-triphosphorique:guanidine phosphotransferase, l'opheline kinase. Biochim. Biophys. Acta 113 (1966) 542-550.
Accepted name: ammonia kinase
Reaction: ATP + NH3 = ADP + phosphoramide
Other names: phosphoramidate-adenosine diphosphate phosphotransferase; phosphoramidate-ADP-phosphotransferase
Systematic name: ATP:ammonia phosphotransferase
Comments: Has a wide specificity. In the reverse direction, N-phosphoglycine and N-phosphohistidine can also act as phosphate donors, and ADP, dADP, GDP, CDP, dTDP, dCDP, IDP and UDP can act as phosphate acceptors (in decreasing order of activity).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-16-3
References:
1. Dowler, M.J. and Nakada, H.I. Yeast phosphoramidate-adenosine diphosphate phosphotransferase. J. Biol. Chem. 243 (1968) 1434-1440. [PMID: 5647264]
Accepted name: phosphoenolpyruvate—protein phosphotransferase
Reaction: phosphoenolpyruvate + protein histidine = pyruvate + protein Nπ-phospho-L-histidine
Other names: phosphoenolpyruvate sugar phosphotransferase enzyme I; phosphopyruvate-protein factor phosphotransferase; phosphopyruvate-protein phosphotransferase; sugar-PEP phosphotransferase enzyme I; phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
Systematic name: phosphoenolpyruvate:protein-L-histidine Nπ-phosphotransferase
Comments: Enzyme I of the phosphotransferase system (cf. EC 2.7.1.69 protein-Nπ-phosphohistidine—sugar phosphotransferase). Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. A similar reaction, where the protein is the enzyme EC 2.7.9.2 pyruvate, water dikinase, is part of the mechanism of that enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-17-4
References:
1. Postma, P.W. and Roseman, S. The bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochim. Biophys. Acta 457 (1976) 213-257. [PMID: 187249]
Accepted name: agmatine kinase
Reaction: ATP + agmatine = ADP + N4-phosphoagmatine
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): phosphagen phosphokinase
Systematic name: ATP:agmatine N4-phosphotransferase
Comments: L-Arginine can act as acceptor, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-75-9
References:
1. Piccinni, E. and Coppellotti, O. Phosphagens in protozoa. II. Presence of phosphagen kinase in Ochramonas danica. Comp. Biochem. Physiol. 62B (1979) 287-289.
[EC 2.7.3.11 Transferred entry: now EC 2.7.13.1, protein-histidine pros-kinase (EC 2.7.3.11 created 1989, deleted 2005)]
[EC 2.7.3.12 Transferred entry: now EC 2.7.13.2, protein-histidine tele-kinase (EC 2.7.3.12 created 1989, deleted 2005)]
Accepted name: glutamine kinase
Reaction: ATP + L-glutamine + H2O = AMP + phosphate + N5-phospho-L-glutamine
Systematic name: ATP:L-glutamine N5-phosphotransferase
Comments: The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Taylor, Z.W., Brown, H.A., Narindoshvili, T., Wenzel, C.Q., Szymanski, C.M., Holden, H.M. and Raushel, F.M. Discovery of a glutamine kinase required for the biosynthesis of the O-methyl phosphoramidate modifications found in the capsular polysaccharides of Campylobacter jejuni. J. Am. Chem. Soc. 139 (2017) 9463-9466. [PMID: 28650156]