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Literature summary for 6.4.1.1 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

Inhibitors Comment Organism Structure
L-cystine
-
Gallus gallus
NEM
-
Gallus gallus
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]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Gallus gallus
-

Substrates and Products (Substrate)

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