ExplorEnz: EC 2.7.4.3

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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]

[EC 2.7.4.3 created 1961]