Enzyme Nomenclature

Continued from EC 2.7.1.151 to EC 2.7.1.226

EC 2.7.2 and EC 2.7.3

Sections

EC 2.7.2 Phosphotransferases with a carboxy group as acceptor
EC 2.7.3 Phosphotransferases with a nitrogenous group as acceptor


EC 2.7.2 Phosphotransferases with a carboxy group as acceptor

Contents

EC 2.7.2.1 acetate kinase
EC 2.7.2.2 carbamate kinase
EC 2.7.2.3 phosphoglycerate kinase
EC 2.7.2.4 aspartate kinase
EC 2.7.2.5 now EC 6.3.4.16
EC 2.7.2.6 formate kinase
EC 2.7.2.7 butyrate kinase
EC 2.7.2.8 acetylglutamate kinase
EC 2.7.2.9 now EC 6.3.5.5
EC 2.7.2.10 phosphoglycerate kinase (GTP)
EC 2.7.2.11 glutamate 5-kinase
EC 2.7.2.12 acetate kinase (diphosphate)
EC 2.7.2.13 glutamate 1-kinase
EC 2.7.2.14 branched-chain-fatty-acid kinase
EC 2.7.2.15 propionate kinase


Entries

EC 2.7.2.1

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]

[EC 2.7.2.1 created 1961, modified 2005]

EC 2.7.2.2

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]

[EC 2.7.2.2 created 1961, modified 2018]

EC 2.7.2.3

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, GTDxpdb.nist.gov/enzyme_thermodynamics/enzyme_compose_query.pl?EC=2.7.2.3, 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.

[EC 2.7.2.3 created 1961]

EC 2.7.2.4

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 2.7.2.4 created 1961]

[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)]

EC 2.7.2.6

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.

[EC 2.7.2.6 created 1965]

EC 2.7.2.7

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.

[EC 2.7.2.7 created 1972, modified 1986, modified 1990]

EC 2.7.2.8

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 2.7.2.8 created 1972]

[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)]

EC 2.7.2.10

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]

[EC 2.7.2.10 created 1976]

EC 2.7.2.11

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]

[EC 2.7.2.11 created 1976]

EC 2.7.2.12

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, 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 2.7.2.12 created 1976]

EC 2.7.2.13

Accepted name: glutamate 1-kinase

Reaction: ATP + L-glutamate = ADP + α-L-glutamyl phosphate

Systematic name: ATP:L-glutamate 1-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80700-24-9

References:

1. Wang, W.-Y., Gough, S.P. and Kannangara, C.G. Biosynthesis of δ-aminolevulinate in greening barley leaves. IV. Isolation of three soluble enzymes required for the conversion of glutamate to δ-aminolevulinate. Carlsberg Res. Commun. 46 (1981) 243-257.

[EC 2.7.2.13 created 1984]

EC 2.7.2.14

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]

[EC 2.7.2.14 created 1990]

EC 2.7.2.15

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.

[EC 2.7.2.15 created 2005]


EC 2.7.3 Phosphotransferases with a nitrogenous group as acceptor

Contents

EC 2.7.3.1 guanidinoacetate kinase
EC 2.7.3.2 creatine kinase
EC 2.7.3.3 arginine kinase
EC 2.7.3.4 taurocyamine kinase
EC 2.7.3.5 lombricine kinase
EC 2.7.3.6 hypotaurocyamine kinase
EC 2.7.3.7 opheline kinase
EC 2.7.3.8 ammonia kinase
EC 2.7.3.9 phosphoenolpyruvate-protein phosphotransferase
EC 2.7.3.10 agmatine kinase
EC 2.7.3.11 now EC 2.7.13.1
EC 2.7.3.12 now EC 2.7.13.2

EC 2.7.3.13 glutamine kinase


Entries

EC 2.7.3.1

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, 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.

[EC 2.7.3.1 created 1961]

EC 2.7.3.2

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.

[EC 2.7.3.2 created 1961]

EC 2.7.3.3

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, GTD, 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.

[EC 2.7.3.3 created 1961]

EC 2.7.3.4

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, 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.

[EC 2.7.3.4 created 1965]

EC 2.7.3.5

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, 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]

[EC 2.7.3.5 created 1965, modified 1976]

EC 2.7.3.6

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.

[EC 2.7.3.6 created 1965]

EC 2.7.3.7

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.

[EC 2.7.3.7 created 1972]

EC 2.7.3.8

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]

[EC 2.7.3.8 created 1972]

EC 2.7.3.9

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]

[EC 2.7.3.9 created 1972]

EC 2.7.3.10

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 2.7.3.10 created 1984]

[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)]

EC 2.7.3.13

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]

[EC 2.7.3.13 created 2017]


Continued with EC 2.7.4.1 to EC 2.7.6.5
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