EC 2.7.4.3 - Adenylate kinase

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IntEnz Enzyme Nomenclature
EC 2.7.4.3

Names

Accepted name:
adenylate kinase
Other names:
5'-AMP-kinase
adenylic kinase
adenylokinase
myokinase
Systematic name:
ATP:AMP phosphotransferase

Reaction

Comments:

Inorganic triphosphate can also act as donor.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00104
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004017
CAS Registry Number: 9013-02-9
UniProtKB/Swiss-Prot: (918) [show] [UniProt]

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 : 3260-3265 (1960).
  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 : 622-629 (1987). [PMID: 3027060]
  3. Noda, L.
    Adenosine triphosphate-adenosine monophosphate transphosphorylase. III. Kinetic studies.
    J. Biol. Chem. 232 : 237-250 (1958).
  4. Noda, L.
    Nucleoside triphosphate-nucleoside monophosphokinases.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes , 2nd ed. vol. 6 , Academic Press , New York , 1962 , 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 : 541-549 (1957).
  6. Noda, L. and Kuby, S.A.
    Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). II. Homogeneity measurements and physicochemical properties.
    J. Biol. Chem. 226 : 551-558 (1957).
  7. Oliver, I.T. and Peel, J.L.
    Myokinase activity in microorganisms.
    Biochim. Biophys. Acta 20 : 390-392 (1956).

[EC 2.7.4.3 created 1961]