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Literature summary for 6.4.1.1 extracted from

  • Attwood, P.V.; Geeves, M.A.
    Changes in catalytic activity and association state of pyruvate carboxylase which are dependent on enzyme concentration (2002), Arch. Biochem. Biophys., 401, 63-72.
    View publication on PubMed
Search for more literature for 6.4.1.1

General Stability

General Stability Organism
upon dilution, there is dissociation of the catalytically active tetrameric enzyme species into inactive dimers. Reactivation of the enzyme results in reassociation of enzymic dimers into tetramers. Gallus gallus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 at high enzyme concentration the enzyme aggregates to form high molecular weight aggregates Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + pyruvate + HCO3- Gallus gallus
-
 ADP + phosphate + oxaloacetate
-
 ?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
29
-
-
 Gallus gallus

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer about 12% of the total enzyme, gel filtration Gallus gallus
monomer about 10% of the total enzyme, gel filtration Gallus gallus
polymer about 4% of the total enzyme elutes as a high molecular weight species, gel filtration Gallus gallus
tetramer about 73% of the total enzyme, gel filtration Gallus gallus