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Literature summary for 2.7.1.40 extracted from

  • Muirhead, H.; Clayden, D.A.; Cuffe, S.P.; Davies, C.
    Crystallographic studies on the structure and catalytic activity of pyruvate kinase from skeletal muscle (1987), Biochem. Soc. Trans., 15, 996-999.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
M1-isozyme, structure Felis catus
skeletal muscle Felis catus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ requirement Felis catus
K+ 1 cation per active site Felis catus
Mg2+ requirement Felis catus
Mg2+ 2 cations per active site Felis catus
Mg2+ pH-dependent Felis catus

Organism

Organism UniProt Comment Textmining
Felis catus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate best nucleoside diphosphate substrate Felis catus ATP + pyruvate
-
ir
CDP + phosphoenolpyruvate less effective than ADP Felis catus CTP + pyruvate
-
?
GDP + phosphoenolpyruvate less effective than ADP Felis catus GTP + pyruvate
-
?
UDP + phosphoenolpyruvate less effective than ADP Felis catus UTP + pyruvate
-
?