Enzyme Nomenclature

Continued from EC 2.7.2 and EC 2.7.3

EC 2.7.4 to EC 2.7.6

Sections

EC 2.7.4 Phosphotransferases with a phosphate group as acceptor
EC 2.7.5 Phosphotransferases with regeneration of donors, apparently catalysing intramolecular transfers
EC 2.7.6 Diphosphotransferases


EC 2.7.4 Phosphotransferases with a phosphate group as acceptor

Contents

EC 2.7.4.1 polyphosphate kinase
EC 2.7.4.2 phosphomevalonate kinase
EC 2.7.4.3 adenylate kinase
EC 2.7.4.4 nucleoside-phosphate kinase
EC 2.7.4.5 deleted, included in EC 2.7.4.14
EC 2.7.4.6 nucleoside-diphosphate kinase
EC 2.7.4.7 phosphomethylpyrimidine kinase
EC 2.7.4.8 guanylate kinase
EC 2.7.4.9 dTMP kinase
EC 2.7.4.10 nucleoside-triphosphate-adenylate kinase
EC 2.7.4.11 (deoxy)adenylate kinase
EC 2.7.4.12 T2-induced deoxynucleotide kinase
EC 2.7.4.13 (deoxy)nucleoside-phosphate kinase
EC 2.7.4.14 UMP/CMP kinase
EC 2.7.4.15 thiamine-diphosphate kinase
EC 2.7.4.16 thiamine-phosphate kinase
EC 2.7.4.17 3-phosphoglyceroyl-phosphate-polyphosphate phosphotransferase
EC 2.7.4.18 farnesyl-diphosphate kinase
EC 2.7.4.19 5-methyldeoxycytidine-5'-phosphate kinase
EC 2.7.4.20 dolichyl-diphosphate-polyphosphate phosphotransferase
EC 2.7.4.21 inositol-hexakisphosphate kinase
EC 2.7.4.22 UMP kinase
EC 2.7.4.23 ribose 1,5-bisphosphate phosphokinase
EC 2.7.4.24 diphosphoinositol-pentakisphosphate kinase
EC 2.7.4.25 (d)CMP kinase
EC 2.7.4.26 isopentenyl phosphate kinase
EC 2.7.4.27 [pyruvate, phosphate dikinase]-phosphate phosphotransferase
EC 2.7.4.28 [pyruvate, water dikinase]-phosphate phosphotransferase
EC 2.7.4.29 Kdo2-lipid A phosphotransferase
EC 2.7.4.30 now EC 2.7.8.43
EC 2.7.4.31 [5-(aminomethyl)furan-3-yl]methyl phosphate kinase
EC 2.7.4.32 farnesyl phosphate kinase

Entries

EC 2.7.4.1

Accepted name: polyphosphate kinase

Reaction: ATP + (phosphate)n = ADP + (phosphate)n+1

Other names: polyphosphoric acid kinase

Systematic name: ATP:polyphosphate phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-44-2

References:

1. Hoffmann-Ostenhof, O., Kenedy, J., Keck, K., Gabriel, O. and Schönfellinger, H.W. En neues Phosphat-übertragendes Ferment aus Hefe. Biochim. Biophys. Acta 14 (1954) 285 only.

2. Kornberg, A., Kornberg, S.R. and Simms, E.S. Metaphosphate synthesis by an enzyme from Escherichia coli. Biochim. Biophys. Acta 20 (1956) 215-227.

3. Muhammed, A. Studies on biosynthesis of polymetaphosphate by an enzyme from Corynebacterium xerosis. Biochim. Biophys. Acta 54 (1961) 121-132.

[EC 2.7.4.1 created 1961]

EC 2.7.4.2

Accepted name: phosphomevalonate kinase

Reaction: ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate

For reaction pathway click here.

Other names: ATP:5-phosphomevalonate phosphotransferase; 5-phosphomevalonate kinase; mevalonate phosphate kinase; mevalonate-5-phosphate kinase; mevalonic acid phosphate kinase

Systematic name: ATP:(R)-5-phosphomevalonate phosphotransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-46-4

References:

1. Bloch, K., Chaykin, S., Phillips, A.H. and de Waard, A. Mevalonic acid pyrophosphate and isopentenyl pyrophosphate. J. Biol. Chem. 234 (1959) 2595-2604.

2. Henning, U., Möslein, E.M. and Lynen, F. Biosynthesis of terpenes. V. Formation of 5-pyrophosphomevalonic acid by phosphomevalonic kinase. Arch. Biochem. Biophys. 83 (1959) 259-267.

3. Levy, G.B. and Popják, G. Studies on the biosynthesis of cholesterol. 10. Mevalonic kinase and phosphomevalonic kinase from liver. Biochem. J. 75 (1960) 417-428.

[EC 2.7.4.2 created 1961]

EC 2.7.4.3

Accepted name: adenylate kinase

Reaction: ATP + AMP = 2 ADP

Other name(s): myokinase; 5'-AMP-kinase; adenylic kinase; adenylokinase

Systematic name: ATP:AMP phosphotransferase

Comments: Inorganic triphosphate can also act as donor.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9013-02-9

References:

1. Chiga, M. and Plaut, G.W.E. Nucleotide transphosphorylases from liver. I. Purification and properties of an adenosine triphosphate-adenosine monophosphate transphosphorylase from swine liver. J. Biol. Chem. 235 (1960) 3260-3265.

2. Saint Girons, I.S., Gilles, A.-M., Margarita, D., Michelson, S., Monnot, M., Fermandjian, S., Danchin, A. and Barzu, O. Structural and catalytic characteristics of Escherichia coli adenylate kinase. J. Biol. Chem. 262 (1987) 622-629. [PMID: 3027060]

3. Noda, L. Adenosine triphosphate-adenosine monophosphate transphosphorylase. III. Kinetic studies. J. Biol. Chem. 232 (1958) 237-250.

4. Noda, L. Nucleoside triphosphate-nucleoside monophosphokinases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp.139-149.

5. Noda, L. and Kuby, S.A. Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). I. Isolation of the crystalline enzyme from rabbit skeletal muscle. J. Biol. Chem. 226 (1957) 541-549.

6. Noda, L. and Kuby, S.A. Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). II. Homogeneity measurements and physicochemical properties. J. Biol. Chem. 226 (1957) 551-558.

7. Oliver, I.T. and Peel, J.L. Myokinase activity in microorganisms. Biochim. Biophys. Acta 20 (1956) 390-392.

[EC 2.7.4.3 created 1961]

EC 2.7.4.4

Accepted name: nucleoside-phosphate kinase

Reaction: ATP + nucleoside phosphate = ADP + nucleoside diphosphate

For diagram of reaction click here.

Other names: NMP-kinase

Systematic name: ATP:nucleoside-phosphate phosphotransferase

Comments: Many nucleotides can act as acceptors; other nucleoside triphosphates can act instead of ATP.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9026-50-0

References:

1. Gibson, D.M., Ayengar, P. and Sanadi, D.R. Transphosphorylations between nucleoside phosphates. Biochim. Biophys. Acta 21 (1956) 86-91.

2. Heppel, L.A., Strominger, J.L. and Maxwell, E.S. Nucleoside monophosphate kinases. II. Transphosphorylation between adenosine monophosphate and nucleotide triphosphate. Biochim. Biophys. Acta 32 (1959) 422-430.

3.Lieberman, I., Kornberg, A. and Simms, E.S. Enzymatic synthesis of nucleotide diphosphates and triphosphates. J. Biol. Chem. 215 (1955) 429-440.

4. Noda, L. Nucleoside triphosphate-nucleoside monophosphokinases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp.139-149.

[EC 2.7.4.4 created 1961]

[EC 2.7.4.5 Deleted entry: deoxycytidylate kinase. Now included with EC 2.7.4.14 cytidylate kinase (EC 2.7.4.5 created 1961, deleted 1972)]

EC 2.7.4.6

Accepted name: nucleoside-diphosphate kinase

Reaction: ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

For diagram of reaction click here.

Other names: nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase

Systematic name: ATP:nucleoside-diphosphate phosphotransferase

Comments: Many nucleoside diphosphates can act as acceptors, while many ribo- and deoxyribonucleoside triphosphates can act as donors.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-51-1

References:

1. Berg, P. and Joklik, W.K. Enzymatic phosphorylation of nucleoside diphosphates. J. Biol. Chem. 210 (1954) 657-672.

2. Gibson, D.M., Ayengar, P. and Sanadi, D.R. Transphosphorylations between nucleoside phosphates. Biochim. Biophys. Acta 21 (1956) 86-91.

3. Kirkland, R.J.A. and Turner, J.F. Nucleoside diphosphokinase of pea seeds. Biochem. J. 72 (1959) 716-720.

4. Krebs, H.A. and Hems, R. Some reactions of adenosine and inosine phosphates in animal tissues. Biochim. Biophys. Acta 12 (1953) 172-180.

5. Nakamura, H. and Sugino, Y. Metabolism of deoxyribonucleotides. 3. Purification and some properties of nucleoside diphosphokinase of calf thymus. J. Biol. Chem. 241 (1966) 4917-4922. [PMID: 5925862]

6. Ratliff, R.L., Weaver, R.H., Lardy, H.A. and Kuby, S.A. Nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). I. Isolation of the crystalline enzyme from brewers' yeast. J. Biol. Chem. 239 (1964) 301-309.

[EC 2.7.4.6 created 1961]

EC 2.7.4.7

Accepted name: phosphooxymethylpyrimidine kinase

Reaction: ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine = ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine

For diagram of reaction click here.

Other name(s): hydroxymethylpyrimidine phosphokinase; ATP:4-amino-2-methyl-5-phosphooxymethylpyrimidine phosphotransferase; ATP:(4-amino-2-methylpyrimidin-5-yl)methyl-phosphate phosphotransferase; phosphomethylpyrimidine kinase

Systematic name: ATP:4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-18-5

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 2.7.4.7 created 1965, modified 2016]

EC 2.7.4.8

Accepted name: guanylate kinase

Reaction: ATP + GMP = ADP + GDP

For diagram of reaction click here.

Other name(s): deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase

Systematic name: ATP:(d)GMP phosphotransferase

Comments: dGMP can also act as acceptor, and dATP can act as donor.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-59-9

References:

1. Buccino, R.J., Jr. and Roth, J.S. Partial purification and properties of ATP:GMP phosphotransferase from rat liver. Arch. Biochem. Biophys. 132 (1969) 49-61. [PMID: 4307347]

2. Hiraga, S. and Sugino, Y. Nucleoside monophosphokinases of Escherichia coli infected and uninfected with an RNA phage. Biochim. Biophys. Acta 114 (1966) 416-418.

3. Griffith, T.J. and Helleiner, C.W. The partial purification of deoxynucleoside monophosphate kinases from L cells. Biochim. Biophys. Acta 108 (1965) 114-124. [PMID: 5862227]

4. Oeschger, M.P. and Bessman, M.J. Purification and properties of guanylate kinase from Escherichia coli. J. Biol. Chem. 241 (1966) 5452-5460. [PMID: 5333666]

5. Shimono, H. and Sugino, Y. Metabolism of deoxyribonucleotides. Purification and properties of deoxyguanosine monophosphokinase of calf thymus. Eur. J. Biochem. 19 (1971) 256-263. [PMID: 5552394]

[EC 2.7.4.8 created 1965]

EC 2.7.4.9

Accepted name: dTMP kinase

Reaction: ATP + dTMP = ADP + dTDP

Other names: thymidine monophosphate kinase; thymidylate kinase; thymidylate monophosphate kinase; thymidylic acid kinase; thymidylic kinase; deoxythymidine 5'-monophosphate kinase; TMPK; thymidine 5'-monophosphate kinase

Systematic name: ATP:dTMP phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-43-1

References:

1. Hurwitz, J. The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material. J. Biol. Chem. 234 (1959) 2351-2358.

2. Keilley, R.K. Purification and properties of thymidine monophosphate kinase from mouse hepatoma. J. Biol. Chem. 245 (1970) 4204-4212. [PMID: 4323166]

3. Nelson, D.J. and Carter, C.E. Purification and characterization of thymidine 5-monophosphate kinase from Escherichia coli B. J. Biol. Chem. 244 (1969) 5254-5262. [PMID: 4899016]

[EC 2.7.4.9 created 1965]

EC 2.7.4.10

Accepted name: nucleoside-triphosphate—adenylate kinase

Reaction: nucleoside triphosphate + AMP = nucleoside diphosphate + ADP

Other names: guanosine triphosphate-adenylate kinase; nucleoside triphosphate-adenosine monophosphate transphosphorylase; GTP:AMP phosphotransferase; isozyme 3 of adenylate kinase

Systematic name: nucleoside-triphosphate:AMP phosphotransferase

Comments: Many nucleoside triphosphates can act as donors.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-74-8

References:

1. Albrecht, G.J. Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria. Biochemistry 9 (1970) 2462-2770. [PMID: 5423264]

2. Chiga, M., Rogers, A.E. and Plaut, G.W.E. Nucleotide transphosphorylases from liver. II. Purification and properties of a 6-oxypurine nucleoside triphosphate-adenosine monophosphate transphosphorylase from swine liver. J. Biol. Chem. 236 (1961) 1800-1805.

[EC 2.7.4.10 created 1965]

EC 2.7.4.11

Accepted name: (deoxy)adenylate kinase

Reaction: ATP + dAMP = ADP + dADP

Systematic name: ATP:(d)AMP phosphotransferase

Comments: AMP can also act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-19-6

References:

1. Griffith, T.J. and Helleiner, C.W. The partial purification of deoxynucleoside monophosphate kinases from L cells. Biochim. Biophys. Acta 108 (1965) 114-124. [PMID: 5862227]

[EC 2.7.4.11 created 1972]

EC 2.7.4.12

Accepted name: T2-induced deoxynucleotide kinase

Reaction: ATP + dGMP (or dTMP) = ADP + dGDP (or dTDP)

Systematic name: ATP:(d)NMP phosphotransferase

Comments: dTMP and dAMP can act as acceptors; dATP can act as donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-99-2

References:

1. Bello, L.J. and Bessman, M.J. The enzymology of virus-infected bacteria. IV. Purification and properties of the deoxynucleotide kinase induced by bacteriophage T2. J. Biol. Chem. 238 (1963) 1777-1787.

[EC 2.7.4.12 created 1972]

EC 2.7.4.13

Accepted name: (deoxy)nucleoside-phosphate kinase

Reaction: ATP + a 2′-deoxyribonucleoside 5′-phosphate = ADP + a 2′-deoxyribonucleoside 5′-diphosphate

Other name(s): deoxynucleoside monophosphate kinase; deoxyribonucleoside monophosphokinase; deoxynucleoside-5′-monophosphate kinase; ATP:deoxynucleoside-phosphate phosphotransferase

Systematic name: ATP:2′-deoxyribonucleoside-5′-phosphate phosphotransferase

Comments: dATP can substitute for ATP.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37278-20-9

References:

1. Bessman, M.J., Herriott, S.T. and Orr, M.J.V.B. The enzymology of virus-infected bacteria. VI. Purification and properties of the deoxynucleotide kinase induced by bacteriophage T5. J. Biol. Chem. 240 (1965) 439-445.

[EC 2.7.4.13 created 1972]

EC 2.7.4.14

Accepted name: UMP/CMP kinase

Reaction: (1) ATP + (d)CMP = ADP + (d)CDP
(2) ATP + UMP = ADP + UDP

Other name(s): cytidylate kinase; deoxycytidylate kinase; CTP:CMP phosphotransferase; dCMP kinase; deoxycytidine monophosphokinase; UMP-CMP kinase; ATP:UMP-CMP phosphotransferase; pyrimidine nucleoside monophosphate kinase; uridine monophosphate-cytidine monophosphate phosphotransferase

Systematic name: ATP:CMP(UMP) phosphotransferase

Comments: This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37278-21-0

References:

1. Hurwitz, J. The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material. J. Biol. Chem. 234 (1959) 2351-2358. [PMID: 14405566]

2. Ruffner, B.W., Jr. and Anderson, E.P. Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis. J. Biol. Chem. 244 (1969) 5994-6002. [PMID: 5350952]

3. Scheffzek, K., Kliche, W., Wiesmuller, L. and Reinstein, J. Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 Å: implications for water-mediated specificity. Biochemistry 35 (1996) 9716-9727. [PMID: 8703943]

4. Zhou, L., Lacroute, F. and Thornburg, R. Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase. Plant Physiol. 117 (1998) 245-254. [PMID: 9576794]

5. Van Rompay, A.R., Johansson, M. and Karlsson, A. Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme. Mol. Pharmacol. 56 (1999) 562-569. [PMID: 10462544]

[EC 2.7.4.14 created 1961 as EC 2.7.4.5, transferred 1972 to EC 2.7.4.14, modified 1980, modified 2011]

EC 2.7.4.15

Accepted name: thiamine-diphosphate kinase

Reaction: ATP + thiamine diphosphate = ADP + thiamine triphosphate

For diagram of reaction click here.

Glossary: thiamine diphosphate

Other names: ATP:thiamin-diphosphate phosphotransferase; TDP kinase; thiamin diphosphate kinase; thiamin diphosphate phosphotransferase; thiamin pyrophosphate kinase; thiamine diphosphate kinase; protein bound thiamin diphosphate:ATP phosphoryltransferase

Systematic name: ATP:thiamine-diphosphate phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-79-0

References:

1. Itokawa, Y. and Cooper, J.R. The enzymatic synthesis of triphosphothiamin. Biochim. Biophys. Acta 158 (1968) 180-182. [PMID: 5661031]

2. Kikuchi, M. and Ikawa, T. Presence of an enzyme mediating transfer of phosphate from thiamine triphosphate to ADP in germinating maize. Bot. Mag. (Tokyo) 97 (1984) 193-205.

[EC 2.7.4.15 created 1972]

EC 2.7.4.16

Accepted name: thiamine-phosphate kinase

Reaction: ATP + thiamine phosphate = ADP + thiamine diphosphate

For diagram of reaction click here.

Glossary: thiamine diphosphate

Other name(s): thiamin-monophosphate kinase; thiamin monophosphatase; thiamin monophosphokinase

Systematic name: ATP:thiamine-phosphate phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-23-9

References:

1. Nishino, H. Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase. J. Biochem. (Tokyo) 72 (1972) 1093-1100. [PMID: 4567662]

[EC 2.7.4.16 created 1976]

EC 2.7.4.17

Accepted name: 3-phosphoglyceroyl-phosphate—polyphosphate phosphotransferase

Reaction: 3-phospho-D-glyceroyl phosphate + (phosphate)n = 3-phosphoglycerate + (phosphate)n+1

Other names: diphosphoglycerate-polyphosphate phosphotransferase; 1,3-diphosphoglycerate-polyphosphate phosphotransferase

Systematic name: 3-phospho-D-glyceroyl-phosphate:polyphosphate phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9055-36-1

References:

1. Kulaev, I.S. and Bobyk, M.A. Detection of a new enzyme in Neurospora crassa - 1,3-diphosphoglycerate:polyphosphatephosphotransferase. Biochemistry (Moscow) 36 (1971) 356-359.

2. Kulaev, I.S., Bobyk, M.A., Nikolaev, N.N., Sergeev, N.S. and Uryson, S.O. Polyphosphate synthesizing enzymes in some fungi and bacteria. Biochemistry (Moscow) 36 (1971) 791-796.

[EC 2.7.4.17 created 1976]

EC 2.7.4.18

Accepted name: farnesyl-diphosphate kinase

Reaction: ATP + farnesyl diphosphate = ADP + farnesyl triphosphate

Other names: farnesyl pyrophosphate kinase

Systematic name: ATP:farnesyl-diphosphate phosphotransferase

Comments: ADP can also act as donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 50936-43-1

References:

1. Schechter, I. Phosphate transfer from trans-farnesyl triphosphate to AMP in Gibberella fujikuroi. Biochim. Biophys. Acta 362 (1974) 233-244. [PMID: 4423368]

[EC 2.7.4.18 created 1978]

EC 2.7.4.19

Accepted name: 5-methyldeoxycytidine-5'-phosphate kinase

Reaction: ATP + 5-methyldeoxycytidine 5'-phosphate = ADP + 5-methyldeoxycytidine diphosphate

Systematic name: ATP:5-methyldeoxycytidine-5'-phosphate phosphotransferase

Comments: The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts m5dCMP into m5dCDP and then into m5dCTP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81032-53-3

References:

1. Wang, R.Y.-H., Huang, L.-H. and Ehrlich, M. A bacteriophage-induced 5-methyldeoxycytidine 5'-monophosphate kinase. Biochim. Biophys. Acta 696 (1982) 31-36. [PMID: 7082669]

[EC 2.7.4.19 created 1984]

[EC 2.7.4.30 Transferred entry: lipid A phosphoethanolamine transferase, now EC 2.7.8.43, lipid A phosphoethanolamine transferase (EC 2.7.4.30 created 2015, deleted 2016)]

EC 2.7.4.21

Accepted name: inositol-hexakisphosphate kinase

Reaction: (1) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
(2) ATP + 1D-myo-inositol 1-diphosphate pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate

Other name(s): ATP:1D-myo-inositol-hexakisphosphate phosphotransferase; IP6K

Systematic name: ATP:1D-myo-inositol-hexakisphosphate 5-phosphotransferase

Comments: Three mammalian isoforms are known to exist.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 176898-37-6

References:

1. Saiardi, A., Erdjument-Bromage, H., Snowman, A.M., Tempst, P. and Snyder, S.H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9 (1999) 1323-1326. [PMID: 10574768]

2. Schell, M.J., Letcher, A.J., Brearley, C.A., Biber, J., Murer, H. and Irvine, R.F. PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase. FEBS Lett. 461 (1999) 169-172. [PMID: 10567691]

3. Albert, C., Safrany, S.T., Bembenek, M.E., Reddy, K.M., Reddy, K.K., Falck, J.-R., Bröcker, M., Shears, S.B. and Mayr, G.W. Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (1997) 553-560. [PMID: 9359429]

4. Lin, H., Fridy, P.C., Ribeiro, A.A., Choi, J.H., Barma, D.K., Vogel, G., Falck, J.R., Shears, S.B., York, J.D. and Mayr, G.W. Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases. J. Biol. Chem. 284 (2009) 1863-1872. [PMID: 18981179]

5. Wang, H., Falck, J.R., Hall, T.M. and Shears, S.B. Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nat. Chem. Biol. 8 (2012) 111-116. [PMID: 22119861]

[EC 2.7.4.21 created 2002 as EC 2.7.1.152, transferred 2003 to EC 2.7.4.21, modified 2013]

EC 2.7.4.22

Accepted name: UMP kinase

Reaction: ATP + UMP = ADP + UDP

Other name(s): uridylate kinase; UMPK; uridine monophosphate kinase; PyrH; UMP-kinase; SmbA

Systematic name: ATP:UMP phosphotransferase

Comments: This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9036-23-1

References:

1. Serina, L., Blondin, C., Krin, E., Sismeiro, O., Danchin, A., Sakamoto, H., Gilles, A.M. and B̢rzu O. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP. Biochemistry 34 (1995) 5066-5074. [PMID: 7711027]

2. Marco-Marin, C., Gil-Ortiz, F. and Rubio, V. The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis. J. Mol. Biol. 352 (2005) 438-454. [PMID: 16095620]

[EC 2.7.4.22 created 2006]

EC 2.7.4.23

Accepted name: ribose 1,5-bisphosphate phosphokinase

Reaction: ATP + α-D-ribose 1,5-bisphosphate = ADP + 5-phospho-α-D-ribose 1-diphosphate

For diagram of reaction click here.

Glossary: PRPP = 5-phospho-α-D-ribose 1-diphosphate

Other name(s): ribose 1,5-bisphosphokinase; PhnN; ATP:ribose-1,5-bisphosphate phosphotransferase

Systematic name: ATP:α-D-ribose-1,5-bisphosphate phosphotransferase

Comments: This enzyme, found in NAD supression mutants of Escherichia coli, synthesizes 5-phospho-α-D-ribose 1-diphosphate (PRPP) without the participation of EC 2.7.6.1, ribose-phosphate diphosphokinase. Ribose, ribose 1-phosphate and ribose 5-phosphate are not substrates, and GTP cannot act as a phosphate donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hove-Jensen, B., Rosenkrantz, T.J., Haldimann, A. and Wanner, B.L. Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways. J. Bacteriol. 185 (2003) 2793-2801. [PMID: 12700258]

[EC 2.7.4.23 created 2006]

EC 2.7.4.24

Accepted name: diphosphoinositol-pentakisphosphate kinase

Reaction: (1) ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
(2) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate

Other name(s): PP-IP5 kinase; diphosphoinositol pentakisphosphate kinase; ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase; PP-InsP5 kinase; PPIP5K; PPIP5K1; PPIP5K2; VIP1; VIP2

Systematic name: ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate phosphotransferase

Comments: This enzyme is activated by osmotic shock [4]. Ins(1,3,4,5,6)P5, 1D-myo-inositol diphosphate tetrakisphosphate and 1D-myo-inositol bisdiphosphate triphosphate are not substrates [4].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Shears, S.B., Ali, N., Craxton, A. and Bembenek, M.E. Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo. J. Biol. Chem. 270 (1995) 10489-10497. [PMID: 7737983]

2. Albert, C., Safrany, S.T., Bembenek, M.E., Reddy, K.M., Reddy, K.K., Falck, J.-R., Bröcker, M., Shears, S.B. and Mayr, G.W. Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (1997) 553-560. [PMID: 9359429]

3. Fridy, P.C., Otto, J.C., Dollins, D.E. and York, J.D. Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases. J. Biol. Chem. 282 (2007) 30754-30762. [PMID: 17690096]

4. Choi, J.H., Williams, J., Cho, J., Falck, J.R. and Shears, S.B. Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that Is activated when cells are exposed to hyperosmotic stress. J. Biol. Chem. 282 (2007) 30763-30775. [PMID: 17702752]

5. Lin, H., Fridy, P.C., Ribeiro, A.A., Choi, J.H., Barma, D.K., Vogel, G., Falck, J.R., Shears, S.B., York, J.D. and Mayr, G.W. Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases. J. Biol. Chem. 284 (2009) 1863-1872. [PMID: 18981179]

6. Wang, H., Falck, J.R., Hall, T.M. and Shears, S.B. Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nat. Chem. Biol. 8 (2012) 111-116. [PMID: 22119861]

[EC 2.7.4.24 created 2003 as EC 2.7.1.155, transferred 2007 to EC 2.7.4.24, modified 2014]

EC 2.7.4.25

Accepted name: (d)CMP kinase

Reaction: ATP + (d)CMP = ADP + (d)CDP

Glossary: CMP = cytidine monophosphate
dCMP = deoxycytidine monophosphate
CDP = cytidine diphosphate
dCDP = deoxycytidine diphosphate
UMP = uridine monophosphate
UDP = uridine diphosphate

Other name(s): prokaryotic cytidylate kinase; deoxycytidylate kinase; dCMP kinase; deoxycytidine monophosphokinase

Systematic name: ATP:(d)CMP phosphotransferase

Comments: The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Bertrand, T., Briozzo, P., Assairi, L., Ofiteru, A., Bucurenci, N., Munier-Lehmann, H., Golinelli-Pimpaneau, B., Barzu, O. and Gilles, A.M. Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. J. Mol. Biol. 315 (2002) 1099-1110. [PMID: 11827479]

2. Thum, C., Schneider, C.Z., Palma, M.S., Santos, D.S. and Basso, L.A. The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP. J. Bacteriol. 191 (2009) 2884-2887. [PMID: 19181797]

[EC 2.7.4.25 created 2011]

EC 2.7.4.26

Accepted name: isopentenyl phosphate kinase

Reaction: ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate

For diagram of reaction click here.

Systematic name: ATP:isopentenyl phosphate phosphotransferase

Comments: The enzyme is involved in the mevalonate pathway in Archaea [1]. The activity has also been identified in the plant Mentha piperita (peppermint) [2]. It is strictly specific for ATP but can use other phosphate acceptors such as dimethylallyl phosphate, geranyl phosphate, or fosfomycin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Grochowski, L.L., Xu, H. and White, R.H. Methanocaldococcus jannaschii uses a modified mevalonate pathway for biosynthesis of isopentenyl diphosphate. J. Bacteriol. 188 (2006) 3192-3198. [PMID: 16621811]

2. Lange, B.M. and Croteau, R. Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step. Proc. Natl. Acad. Sci. USA 96 (1999) 13714-13719. [PMID: 10570138]

3. Chen, M. and Poulter, C.D. Characterization of thermophilic archaeal isopentenyl phosphate kinases. Biochemistry 49 (2010) 207-217. [PMID: 19928876]

4. Mabanglo, M.F., Schubert, H.L., Chen, M., Hill, C.P. and Poulter, C.D. X-ray structures of isopentenyl phosphate kinase. ACS Chem. Biol. 5 (2010) 517-527. [PMID: 20402538]

[EC 2.7.4.26 created 2012]

EC 2.7.4.27

Accepted name: [pyruvate, phosphate dikinase]-phosphate phosphotransferase

Reaction: [pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate

Other name(s): PPDK regulatory protein (ambiguous); pyruvate, phosphate dikinase regulatory protein (ambiguous); bifunctional dikinase regulatory protein (ambiguous); PDRP1 (gene name)

Systematic name: [pyruvate, phosphate dikinase] phosphate:phosphate phosphotransferase

Comments: The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyses the phosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.11.32, [pyruvate, phosphate dikinase] kinase [2-5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Burnell, J.N. and Hatch, M.D. Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase. Arch. Biochem. Biophys. 231 (1984) 175-182. [PMID: 6326674]

2. Burnell, J.N. and Hatch, M.D. Regulation of C4 photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase. Arch. Biochem. Biophys. 237 (1985) 490-503. [PMID: 2983615]

3. Chastain, C.J., Botschner, M., Harrington, G.E., Thompson, B.J., Mills, S.E., Sarath, G. and Chollet, R. Further analysis of maize C4 pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues. Arch. Biochem. Biophys. 375 (2000) 165-170. [PMID: 10683263]

4. Burnell, J.N. and Chastain, C.J. Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene. Biochem. Biophys. Res. Commun. 345 (2006) 675-680. [PMID: 16696949]

5. Chastain, C.J., Xu, W., Parsley, K., Sarath, G., Hibberd, J.M. and Chollet, R. The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure. Plant J. 53 (2008) 854-863. [PMID: 17996018]

[EC 2.7.4.27 created 2012]

EC 2.7.4.28

Accepted name: [pyruvate, water dikinase]-phosphate phosphotransferase

Reaction: [pyruvate, water dikinase] phosphate + phosphate = [pyruvate, water dikinase] + diphosphate

Other name(s): PSRP (ambiguous)

Systematic name: [pyruvate, water dikinase] phosphate:phosphate phosphotransferase

Comments: The enzyme from the bacterium Escherichia coli is bifunctional and catalyses both the phosphorylation and dephosphorylation of EC 2.7.9.2, pyruvate, water dikinase. cf. EC 2.7.11.33, [pyruvate, water dikinase] kinase [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Burnell, J.N. Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria. BMC Biochem. 11 (2010) 1. [PMID: 20044937]

[EC 2.7.4.28 created 2012]

EC 2.7.4.29

Accepted name: Kdo2-lipid A phosphotransferase

Reaction: ditrans-octacis-undecaprenyl diphosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A = ditrans-octacis-undecaprenyl phosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A 1-diphosphate

Glossary: lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A 1-diphosphate =
2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl diphosphate

Other name(s): lipid A undecaprenyl phosphotransferase; LpxT; YeiU

Systematic name: ditrans-octacis-undecaprenyl diphosphate:α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid-A phosphotransferase

Comments: An inner-membrane protein. The activity of the enzyme is regulated by PmrA. In vitro the enzyme can use diacylglycerol 3-diphosphate as the phosphate donor.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Touze, T., Tran, A.X., Hankins, J.V., Mengin-Lecreulx, D. and Trent, M.S. Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate. Mol. Microbiol. 67 (2008) 264-277. [PMID: 18047581]

2. Herrera, C.M., Hankins, J.V. and Trent, M.S. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol. Microbiol. 76 (2010) 1444-1460. [PMID: 20384697]

[EC 2.7.4.29 created 2015]

EC 2.7.4.30

Accepted name: lipid A phosphoethanolamine transferase

Reaction: (1) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
(2) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
(3) diacylphosphatidylethanolamine + lipid A 1-(2-aminoethyl diphosphate) = diacylglycerol + lipid A 1,4'-bis(2-aminoethyl diphosphate)

Glossary: lipid A (Campylobacter jejuni) = 2,3-dideoxy-2,3-bis[(3R)-3-(hexadecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A (Escherichia coli) = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A (Helicobacter pylori) = 2-deoxy-2-[(3R)-3-(octadecanoyloxy)octadecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyhexadecanoyl]-2-[(3R)-3-hydroxyoctadecanamido]-α-D-glucopyranosyl phosphate
lipid A (Neisseria meningitidis) = 2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid A 1-[(2-aminoethyl) diphosphate] = P1-(2-aminoethyl) P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate
lipid A 1,4'-bis(2-aminoethyl diphosphate) = P1-(2-aminoethyl) P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-(2-aminoethyldiphospho)-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate

Other name(s): lipid A PEA transferase; PmrA; LptA

Systematic name: diacylphosphatidylethanolamine:lipid-A phosphoethanolaminetransferase

Comments: The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-β-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Tran, A.X., Karbarz, M.J., Wang, X., Raetz, C.R., McGrath, S.C., Cotter, R.J. and Trent, M.S. Periplasmic cleavage and modification of the 1-phosphate group of Helicobacter pylori lipid A. J. Biol. Chem. 279 (2004) 55780-55791. [PMID: 15489235]

2. Herrera, C.M., Hankins, J.V. and Trent, M.S. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol. Microbiol. 76 (2010) 1444-1460. [PMID: 20384697]

3. Cullen, T.W. and Trent, M.S. A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium Campylobacter jejuni. Proc. Natl. Acad. Sci. USA 107 (2010) 5160-5165. [PMID: 20194750]

4. Anandan, A., Piek, S., Kahler, C.M. and Vrielink, A. Cloning, expression, purification and crystallization of an endotoxin-biosynthesis enzyme from Neisseria meningitidis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 (2012) 1494-1497. [PMID: 23192031]

5. Wanty, C., Anandan, A., Piek, S., Walshe, J., Ganguly, J., Carlson, R.W., Stubbs, K.A., Kahler, C.M. and Vrielink, A. The structure of the neisserial lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin. J. Mol. Biol. 425 (2013) 3389-3402. [PMID: 23810904]

[EC 2.7.4.30 created 2015]

EC 2.7.4.31

Accepted name: [5-(aminomethyl)furan-3-yl]methyl phosphate kinase

Reaction: ATP + [5-(aminomethyl)furan-3-yl]methyl phosphate = ADP + [5-(aminomethyl)furan-3-yl]methyl diphosphate

For diagram of reaction click here.

Other name(s): MfnE

Systematic name: ATP:[5-(aminomethyl)furan-3-yl]methyl-phosphate phosphotransferase

Comments: Requires Mg2+. The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran cofactor.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wang, Y., Xu, H., Jones, M.K. and White, R.H. Identification of the final two genes functioning in methanofuran biosynthesis in Methanocaldococcus jannaschii. J. Bacteriol. 197 (2015) 2850-2858. [PMID: 26100040]

[EC 2.7.4.31 created 2015]

EC 2.7.4.32

Accepted name: farnesyl phosphate kinase

Reaction: CTP + (2E,6E)-farnesyl phosphate = CDP + (2E,6E)-farnesyl diphosphate

For diagram of reaction click here.

Systematic name: CTP:(2E,6E)-farnesyl-phosphate phosphotransferase

Comments: The enzyme, found in plants and animals, is specific for CTP as phosphate donor. It does not use farnesol as substrate (cf. EC 2.7.1.216, farnesol kinase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bentinger, M., Grunler, J., Peterson, E., Swiezewska, E. and Dallner, G. Phosphorylation of farnesol in rat liver microsomes: properties of farnesol kinase and farnesyl phosphate kinase. Arch. Biochem. Biophys. 353 (1998) 191-198. [PMID: 9606952]

2. Fitzpatrick, A.H., Bhandari, J. and Crowell, D.N. Farnesol kinase is involved in farnesol metabolism, ABA signaling and flower development in Arabidopsis. Plant J. 66 (2011) 1078-1088. [PMID: 21395888]

[EC 2.7.4.32 created 2017]


EC 2.7.5 Phosphotransferases with regeneration of donors, apparently catalysing intramolecular transfers

EC 2.7.5 In the early editions of Enzyme Nomenclature, phosphomutases were listed here under the heading 'Phosphotransferases with regeneration of donors, apparently catalysing intramolecular transfers'. They are now listed in sub-subgroup 5.4.2 on the basis of the overall isomerization reaction.

[EC 2.7.5.1 Transferred entry: now EC 5.4.2.2 phosphoglucomutase (EC 2.7.5.1 created 1961, deleted 1984)]

[EC 2.7.5.2 Transferred entry: now EC 5.4.2.3 phosphoacetylglucosamine mutase (EC 2.7.5.2 created 1961, deleted 1984)]

[EC 2.7.5.3 Transferred entry: now EC 5.4.2.1 phosphoglyceromutase (EC 2.7.5.3 created 1961, deleted 1984)]

[EC 2.7.5.4 Transferred entry: now EC 5.4.2.4 bisphosphoglyceromutase (EC 2.7.5.4 created 1961, deleted 1984)]

[EC 2.7.5.5 Transferred entry: now EC 5.4.2.5 phosphoglucomutase (glucose-cofactor) (EC 2.7.5.5 created 1972, deleted 1984)]

[EC 2.7.5.6 Transferred entry: now EC 5.4.2.7 phosphopentomutase (EC 2.7.5.6 created 1972, deleted 1984)]

[EC 2.7.5.7 Transferred entry: now EC 5.4.2.8 phosphomannomutase (EC 2.7.5.7 created 1981, deleted 1984)]


EC 2.7.6 Diphosphotransferases

Contents

EC 2.7.6.1 ribose-phosphate diphosphokinase
EC 2.7.6.2 thiamine diphosphokinase
EC 2.7.6.3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
EC 2.7.6.4 nucleotide diphosphokinase
EC 2.7.6.5 GTP diphosphokinase


Entries

EC 2.7.6.1

Accepted name: ribose-phosphate diphosphokinase

Reaction: ATP + D-ribose 5-phosphate = AMP + 5-phospho-α-D-ribose 1-diphosphate

For diagram of reaction click here.

Glossary: PRPP = 5-phospho-α-D-ribose 1-diphosphate

Other name(s): ribose-phosphate pyrophosphokinase; PRPP synthetase; phosphoribosylpyrophosphate synthetase; PPRibP synthetase; PP-ribose P synthetase; 5-phosphoribosyl-1-pyrophosphate synthetase; 5-phosphoribose pyrophosphorylase; 5-phosphoribosyl-alpha-1-pyrophosphate synthetase; phosphoribosyl-diphosphate synthetase; phosphoribosylpyrophosphate synthase; pyrophosphoribosylphosphate synthetase; ribophosphate pyrophosphokinase; ribose-5-phosphate pyrophosphokinase

Systematic name: ATP:D-ribose-5-phosphate diphosphotransferase

Comments: dATP can also act as donor.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9015-83-2

References:

1. Hughes, D.E. and Williamson, D.H. Some properties of glutaminase of Clostridium welchii. Biochem. J. 51 (1952) 45-55.

2. Hurlbert, R.B. and Reichard, P. The conversion of orotic acid to uridine nucleotides in vitro. Acta Chem. Scand. 9 (1955) 251-262.

3. Remy, C.N., Remy, W.T. and Buchanan, J.M. Biosynthesis of the purines. VIII. Enzymatic synthesis and utilization of α-5-phosphoribosylpyrophosphate. J. Biol. Chem. 217 (1955) 885-895.

4. Switzer, R.L. Regulation and mechanism of phosphoribosylpyrophosphate synthetase. I. Purification and properties of the enzyme from Salmonella typhimurium. J. Biol. Chem. 244 (1969) 2854-2863. [PMID: 4306285]

[EC 2.7.6.1 created 1961]

EC 2.7.6.2

Accepted name: thiamine diphosphokinase

Reaction: ATP + thiamine = AMP + thiamine diphosphate

Glossary: thiamine diphosphate

Other name(s): thiamin kinase; thiamine pyrophosphokinase; ATP:thiamin pyrophosphotransferase; thiamin pyrophosphokinase; thiamin pyrophosphotransferase; thiaminokinase; thiamin:ATP pyrophosphotransferase; TPTase

Systematic name: ATP:thiamine diphosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-24-8

References:

1. Leuthardt, F. and Nielsen, H. Phosphorylation biologique de la thiamine. Helv. Chim. Acta 35 (1952) 1196-1209.

2. Shimazono, N., Mano, Y., Tanaka, R. and Kajiro, Y. Mechanism of transpyrophosphorylation with thiamine pyrophosphokinase. J. Biochem. (Tokyo) 46 (1959) 959-961.

3. Steyn-Parvé, E.P. Partial purification and properties of thiaminokinase from yeast. Biochim. Biophys. Acta 8 (1952) 310-324.

[EC 2.7.6.2 created 1961]

EC 2.7.6.3

Accepted name: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase

Reaction: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + (7,8-dihydropterin-6-yl)methyl diphosphate

For diagram of reaction click here or click here.

Other name(s): 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; H2-pteridine-CH2OH pyrophosphokinase; 7,8-dihydroxymethylpterin-pyrophosphokinase; HPPK; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hydroxymethyldihydropteridine pyrophosphokinase; ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase

Systematic name: ATP:6-hydroxymethyl-7,8-dihydropterin 6'-diphosphotransferase

Comments: Binds 2 Mg2+ ions that are essential for activity [4]. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase [4], the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase [7], while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities [6].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-23-2

References:

1. Shiota, T., Baugh, C.M., Jackson, R. and Dillard, R. The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate. Biochemistry 8 (1969) 5022-5028. [PMID: 4312465]

2. Richey, D.P. and Brown, G.M. The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid. J. Biol. Chem. 244 (1969) 1582-1592. [PMID: 4304228]

3. Richey, D.P. and Brown, G.M. Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate synthetase from Escherichia coli. Methods Enzymol. 18B (1971) 765-771.

4. Lopez, P. and Lacks, S.A. A bifunctional protein in the folate biosynthetic pathway of Streptococcus pneumoniae with dihydroneopterin aldolase and hydroxymethyldihydropterin pyrophosphokinase activities. J. Bacteriol. 175 (1993) 2214-2220. [PMID: 8385663]

5. Blaszczyk, J., Shi, G., Yan, H. and Ji, X. Catalytic center assembly of HPPK as revealed by the crystal structure of a ternary complex at 1.25 Å resolution. Structure 8 (2000) 1049-1058. [PMID: 11080626]

6. Güldener, U., Koehler, G.J., Haussmann, C., Bacher, A., Kricke, J., Becher, D. and Hegemann, J.H. Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth. Mol. Biol. Cell 15 (2004) 3811-3828. [PMID: 15169867]

7. Storozhenko, S., Navarrete, O., Ravanel, S., De Brouwer, V., Chaerle, P., Zhang, G.F., Bastien, O., Lambert, W., Rebeille, F. and Van Der Straeten, D. Cytosolic hydroxymethyldihydropterin pyrophosphokinase/dihydropteroate synthase from Arabidopsis thaliana: a specific role in early development and stress response. J. Biol. Chem. 282 (2007) 10749-10761. [PMID: 17289662]

[EC 2.7.6.3 created 1972, modified 2015]

EC 2.7.6.4

Accepted name: nucleotide diphosphokinase

Reaction: ATP + nucleoside 5'-phosphate = AMP + 5'-phosphonucleoside 3'-diphosphate

Other name(s): nucleotide pyrophosphokinase; ATP:nucleotide pyrophosphotransferase; ATP nucleotide 3'-pyrophosphokinase; nucleotide 3'-pyrophosphokinase

Systematic name: ATP:nucleoside-5'-phosphate diphosphotransferase

Comments: The enzyme acts on the 5'-mono-, di- and triphosphate derivatives of purine nucleosides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 53167-92-3

References:

1. Murao, S. and Nishino, T. Isolation and identification of ATP:nucleotide pyrophosphotransferase-producing microorganism. Agric. Biol. Chem. 38 (1974) 2483-2489.

2. Nishino, T. and Murao, S. Purification and some properties of ATP:nucleotide pyrophosphotransferase of Streptomyces adephospholyticus. Agric. Biol. Chem. 38 (1974) 2491-2496.

3. Nishino, T. and Murao, S. Characterization of pyrophosphoryl transfer reaction of ATP:nucleotide pyrophosphotransferase. Agric. Biol. Chem. 39 (1975) 1007-1014.

[EC 2.7.6.4 created 1976]

EC 2.7.6.5

Accepted name: GTP diphosphokinase

Reaction: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate

Other name(s): stringent factor; guanosine 3',5'-polyphosphate synthase; GTP pyrophosphokinase; ATP-GTP 3'-diphosphotransferase; guanosine 5',3'-polyphosphate synthetase; (p)ppGpp synthetase I; (p)ppGpp synthetase II; guanosine pentaphosphate synthetase; GPSI; GPSII

Systematic name: ATP:GTP 3'-diphosphotransferase

Comments: GDP can also act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 63690-89-1

References:

1. Fehr, S. and Richter, D. Stringent response of Bacillus stearothermophilus: evidence for the existence of two distinct guanosine 3',5'-polyphosphate synthetases. J. Bacteriol. 145 (1981) 68-73. [PMID: 6161916]

2. Sy, J. and Akers, H. Purification and properties of guanosine 5',3'-polyphosphate synthetase from Bacillus brevis. Biochemistry 15 (1976) 4399-4403. [PMID: 184817]

[EC 2.7.6.5 created 1981]


Continued with EC 2.7.7.1 to EC 2.7.7.58
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