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. [PMID: 13693070] |
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. [PMID: 13549414] |
4. |
Noda, L. Nucleoside triphosphate-nucleoside monophosphokinases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), 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. [PMID: 13428784] |
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. [PMID: 13428785] |
7. |
Oliver, I.T. and Peel, J.L. Myokinase activity in microorganisms. Biochim. Biophys. Acta 20 (1956) 390–392. [DOI] [PMID: 13328866] |
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[EC 2.7.4.3 created 1961] |
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EC
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2.7.4.30
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Transferred entry: | lipid A phosphoethanolamine transferase. Now EC 2.7.8.43, lipid A phosphoethanolamine transferase
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[EC 2.7.4.30 created 2015, deleted 2016] |
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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 |
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For diagram of methanofuran biosynthesis, 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 |
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. [DOI] [PMID: 26100040] |
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[EC 2.7.4.31 created 2015] |
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EC |
2.7.4.32 |
Accepted name: |
farnesyl phosphate kinase |
Reaction: |
CTP + (2E,6E)-farnesyl phosphate = CDP + (2E,6E)-farnesyl diphosphate |
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For diagram of acyclic sesquiterpenoid biosynthesis, 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 |
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. [DOI] [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. [DOI] [PMID: 21395888] |
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[EC 2.7.4.32 created 2017] |
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EC |
2.7.4.33 |
Accepted name: |
AMP-polyphosphate phosphotransferase |
Reaction: |
ADP + (phosphate)n = AMP + (phosphate)n+1 |
Other name(s): |
PA3455 (locus name); PPK2D; PAP |
Systematic name: |
ADP:polyphosphate phosphotransferase |
Comments: |
The enzyme, characterized from the bacteria Acinetobacter johnsonii and Pseudomonas aeruginosa, transfers a phosphate group from polyphosphates to nucleotide monophosphates. The highest activity is achieved with AMP, but the enzyme can also phosphorylate GMP, dAMP, dGMP, IMP, and XMP. The reverse reactions were not detected. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Bonting, C.F., Kortstee, G.J. and Zehnder, A.J. Properties of polyphosphate: AMP phosphotransferase of Acinetobacter strain 210A. J. Bacteriol. 173 (1991) 6484–6488. [PMID: 1655714] |
2. |
Shiba, T., Itoh, H., Kameda, A., Kobayashi, K., Kawazoe, Y. and Noguchi, T. Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent nucleoside monophosphate kinase in Acinetobacter johnsonii 210A. J. Bacteriol. 187 (2005) 1859–1865. [PMID: 15716459] |
3. |
Nocek, B., Kochinyan, S., Proudfoot, M., Brown, G., Evdokimova, E., Osipiuk, J., Edwards, A.M., Savchenko, A., Joachimiak, A. and Yakunin, A.F. Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. Proc. Natl. Acad. Sci. USA 105 (2008) 17730–17735. [PMID: 19001261] |
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[EC 2.7.4.33 created 2020] |
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EC |
2.7.4.34 |
Accepted name: |
GDP-polyphosphate phosphotransferase |
Reaction: |
GTP + (phosphate)n = GDP + (phosphate)n+1 |
Other name(s): |
ppk2 (gene name); polyphosphate kinase 2 |
Systematic name: |
GTP:polyphosphate phosphotransferase |
Comments: |
Polyphosphate kinase 2, characterized from the bacterium Pseudomonas aeruginosa, uses inorganic polyphosphate as a donor to convert GDP to GTP. The enzyme can also act on ADP (cf. EC 2.7.4.1, ATP-polyphosphate phosphotransferase), but with lower activity. The enzyme has only a trivial activity in the opposite direction (synthesizing polyphosphate from GTP). The GTP that is produced is believed to be consumed by EC 2.7.7.13, mannose-1-phosphate guanylyltransferase, for production of alginate during stationary phase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Zhang, H., Ishige, K. and Kornberg, A. A polyphosphate kinase (PPK2) widely conserved in bacteria. Proc. Natl. Acad. Sci. USA 99 (2002) 16678–16683. [DOI] [PMID: 12486232] |
2. |
Ishige, K., Zhang, H. and Kornberg, A. Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP. Proc. Natl. Acad. Sci. USA 99 (2002) 16684–16688. [DOI] [PMID: 12482933] |
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[EC 2.7.4.34 created 2021] |
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