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Literature summary for 6.4.1.1 extracted from

  • Branson, J.P.; Nezic, M.; Wallace, J.C.; Attwood, P.V.
    Kinetic characterization of yeast pyruvate carboxylase isozyme pyc1 (2002), Biochemistry, 41, 4459-4466.
    View publication on PubMed
Search for more literature for 6.4.1.1

Activating Compound

Activating Compound Comment Organism Structure
acetyl-CoA activates Pyc1 at 0.25 mM Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.056
-
 ATP pH 7.8, 30°C, wild-type Pyc1 Saccharomyces cerevisiae
0.495
-
 pyruvate pH 7.8, 30°C, wild-type Pyc1 Saccharomyces cerevisiae
1.36
-
 HCO3- pH 7.8, 30°C, wild-type Pyc1 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Saccharomyces cerevisiae 5737
-

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Pyc1 isoform, 88% purity Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
quarternary structure is quite stable in absence o acetyl-CoA Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + carbamoyl phosphate
-
 Saccharomyces cerevisiae ATP + ?
-
 ?
ATP + pyruvate + HCO3-
-
 Saccharomyces cerevisiae ADP + phosphate + oxaloacetate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.014
-
 ATP pH 7.8, 30°C, ATP cleavage in absence of acetyl-CoA Saccharomyces cerevisiae
0.037
-
 ATP pH 7.8, 30°C, ATP cleavage in presence of acetyl-CoA Saccharomyces cerevisiae