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Literature summary extracted from

  • Stammers, d.H.; Levine, M.; Stuart, D.I.; Muirhead, H.
    Structure of cat muscle pyruvate kinase at 0.26 nm resolution (1977), Biochem. Soc. Trans., 5, 654-657.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.40 3-dimensional structure of M-type isozyme Felis catus
2.7.1.40 skeletal muscle Felis catus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.40 divalent cation requirement Felis catus
2.7.1.40 divalent cation requires both a divalent and a monovalent cation Felis catus
2.7.1.40 monovalent cation requirement Felis catus
2.7.1.40 monovalent cation requires both a divalent and a monovalent cation Felis catus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.40 additional information
-
 3-dimensional structure of cat M-type isozyme Felis catus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.40 Felis catus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.40 ATP + pyruvate = ADP + phosphoenolpyruvate catalyzes the addition of a proton and the loss of a phosphoryl group which is transferred to ADP Felis catus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.40 ADP + phosphoenolpyruvate catalyzes the addition of a proton and the loss of a phosphoryl group which is transferred to ADP Felis catus ATP + pyruvate
-
 ir

Subunits

EC Number Subunits Comment Organism
2.7.1.40 tetramer
-
 Felis catus