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Literature summary for 6.4.1.1 extracted from

  • Huberts, D.H.; Venselaar, H.; Vriend, G.; Veenhuis, M.; van der Klei, I.J.
    The moonlighting function of pyruvate carboxylase resides in the non-catalytic end of the TIM barrel (2010), Biochim. Biophys. Acta, 1803, 1038-1042.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y542V/A557Q/S762D the triple mutation fully inactivates the moonlighting function of Pyc1, but not the enzyme activity of pyruvate carboxylase Ogataea angusta

Organism

Organism UniProt Comment Textmining
Ogataea angusta
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate + HCO3- + H+
-
Ogataea angusta ADP + oxaloacetate + phosphate
-
?

Synonyms

Synonyms Comment Organism
Pyc1
-
Ogataea angusta

Cofactor

Cofactor Comment Organism Structure
ATP
-
Ogataea angusta

General Information

General Information Comment Organism
physiological function pyruvate carboxylase protein is required for import and assembly of the peroxisomal enzyme alcohol oxidase Ogataea angusta