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Literature summary for 6.4.1.1 extracted from

  • Gurr, J.A.; Jones, K.M.
    Purification and characterization of pyruvate carboxylase from Arthrobacter globiformis (1977), Arch. Biochem. Biophys., 179, 444-455.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
acetyl-CoA activates Arthrobacter globiformis
acetyl-CoA in absence of acetyl-CoA the maximal rate of oxaloacetate synthesis is 4% of that obtained in presence of saturating concentrations of acetyl-CoA Arthrobacter globiformis

General Stability

General Stability Organism
acetyl-CoA and sodium pyruvate protects against cold inactivation. L-Asp decreases inactivation, 1 M sucrose gives complete protection Arthrobacter globiformis
the presence of KCl at 10, 20, 50, and 100 mM potassium phosphate buffer-KCl buffer at 0°C leads to 85%, 44%, 17% and 0% loss of activity Arthrobacter globiformis

Inhibitors

Inhibitors Comment Organism Structure
Avidin
-
Arthrobacter globiformis
L-Asp
-
Arthrobacter globiformis
Na+ slight Arthrobacter globiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.08
-
ATP
-
Arthrobacter globiformis
0.33
-
HCO3-
-
Arthrobacter globiformis
1.86
-
pyruvate
-
Arthrobacter globiformis

Metals/Ions

Metals/Ions Comment Organism Structure
K+ increases activity by a maximum of 27% at 70 mM Arthrobacter globiformis
Mg2+ activates Arthrobacter globiformis
Mg2+ Km: 0.7 mM Arthrobacter globiformis
NH4+ increases activity by a maximum of 39% at 80 mM Arthrobacter globiformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
4 * 130000, SDS-PAGE Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Arthrobacter globiformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
27
-
-
Arthrobacter globiformis

Storage Stability

Storage Stability Organism
0°C, 10 mM potassium phosphate, 10 mM KCl, 1 mM EDTA, 0.1 mM DTT, pH 6.8, potassium phosphate-KCl buffer, 50% loss of activity after 10 min Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate + HCO3-
-
Arthrobacter globiformis ADP + phosphate + oxaloacetate
-
?
ATP + pyruvate + HCO3- ATP in form of MgATP2- Arthrobacter globiformis ADP + phosphate + oxaloacetate
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 130000, SDS-PAGE Arthrobacter globiformis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
cold inactivation Arthrobacter globiformis
-
-
10 mM potassium phosphate, 10 mM KCl, 1 mM EDTA, 0.1 mM DTT, pH 6.8, potassium phosphate-KCl buffer, 50% loss of activity after 10 min Arthrobacter globiformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.6
-
in presence of 5 mM Mn2+ Arthrobacter globiformis
7.6
-
in presence of 5 mM Mg2+ Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
biotin enzyme contains biotin Arthrobacter globiformis