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Literature summary for 2.7.1.40 extracted from

  • Murakami, K.; Tsubouchi, R.; Fukayama, M.; Qiao, S.; Yoshino, M.
    Iron-dependent oxidative inactivation with affinity cleavage of pyruvate kinase (2009), Biol. Trace Elem. Res., 130, 31-38.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ascorbate treatment of rabbit muscle pyruvate kinase with 10 mM ascorbate causes an inactivation with the cleavage of peptide bond. The inactivation or fragmentation of the enzyme is prevented by addition of Mg2+, catalase, and mannitol, but ADP and PEP the substrates do not show any effect Oryctolagus cuniculus
FeSO4 treatment of rabbit muscle pyruvate kinase with 0.02 mM FeSO4 causes an inactivation with the cleavage of peptide bond. The inactivation or fragmentation of the enzyme is prevented by addition of Mg2+, catalase, and mannitol, but ADP and PEP the substrates do not show any effect Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ addition of Mg2+ protects the enzyme completely from the ferrous ion-mediated inactivation Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57900
-
native enzyme, MALDI-TOF mass spectrometry Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate
-
Oryctolagus cuniculus ATP + pyruvate
-
?

Cofactor

Cofactor Comment Organism Structure
ADP
-
Oryctolagus cuniculus