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.