The Enzyme Database

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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. (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. [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]
[EC 2.7.4.3 created 1961]
 
 
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 2.7.4.31     
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 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]
[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 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]
[EC 2.7.4.32 created 2017]
 
 


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