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Literature summary for 6.3.4.14 extracted from

  • Yu, L.P.; Xiang, S.; Lasso, G.; Gil, D.; Valle, M.; Tong, L.
    A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A (2009), Structure, 17, 823-832.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
acetyl-CoA allosteric activator of holoenzyme. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with acetyl-CoA. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus A0A0H3JUV1 component of pyruvate carboxylase
-

Synonyms

Synonyms Comment Organism
biotin carboxylase component of pyruvate carboxylase Staphylococcus aureus