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Literature summary extracted from

  • Palacian, E.; Neet, K.E.
    Pyruvate carboxylase: inactivation by sulfhydryl group reagents in the presence of certain inorganic anions, substrates, and modifiers and the effects on the allosteric properties of the enzyme (1972), Biochim. Biophys. Acta, 276, 297-312.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.4.1.1 L-cystine
-
 Gallus gallus
6.4.1.1 NEM
-
 Gallus gallus
6.4.1.1 sulfhydryl reagents effects of ATP, acetyl-CoA, and oxalacetate on the rates of inactivation of pyruvate carboxylase by sulfhydryl reagents depend upon the anion present, the reagent used, and the phase of inactivation considered. Protection by acetyl-CoA is cooperative Gallus gallus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4.1.1 0.33
-
 HCO3- MgATP2- Gallus gallus
6.4.1.1 0.48
-
 pyruvate
-
 Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.4.1.1 Mg2+ activates Gallus gallus
6.4.1.1 Mg2+ Km: 0.3 mM Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.1 Gallus gallus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.4.1.1 liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.1 ATP + pyruvate + HCO3-
-
 Gallus gallus ADP + phosphate + oxaloacetate
-
 ?