Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.40 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)

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Felis catus
-
-
-

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits Comment Organism
tetramer
-
Felis catus