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Literature summary extracted from

  • Westerhold, L.E.; Bridges, L.C.; Shaikh, S.R.; Zeczycki, T.N.
    Kinetic and thermodynamic analysis of acetyl-CoA activation of Staphylococcus aureus pyruvate carboxylase (2017), Biochemistry, 56, 3492-3506 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.4.1.1 acetyl-CoA the substrates of the biotin carboxylase and carboxyl transferase domain are energetically coupled in the presence of acetyl-CoA. Both kinetic and energetic coupling between the two domains is lost in the absence of acetyl-CoA Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.1 Staphylococcus aureus A0A0H3JRU9
-
-
6.4.1.1 Staphylococcus aureus ATCC 700699 A0A0H3JRU9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.1 additional information thermodynamic activation parameters for the pyruvate carboxylase-catalyzed carboxylation of pyruvate are largely independent of acetyl-CoA Staphylococcus aureus ?
-
 ?
6.4.1.1 additional information thermodynamic activation parameters for the pyruvate carboxylase-catalyzed carboxylation of pyruvate are largely independent of acetyl-CoA Staphylococcus aureus ATCC 700699 ?
-
 ?