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Literature summary for 6.4.1.3 extracted from

  • Kaziro, Y.; Ochoa, S.; Warner, R.C.; Chen, J.Y.
    Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase (1961), J. Biol. Chem., 236, 1917-1923.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 propanoyl-CoA
-
 Sus scrofa
1.5
-
 butanoyl-CoA
-
 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
690000
-
 calculation from sedimentation and diffusion data Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.6
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetyl-CoA + HCO3- at 0.7% of the velocity compared to propanoyl-CoA Sus scrofa ADP + phosphate + malonyl-CoA
-
 ?
ATP + butanoyl-CoA + HCO3- at 5.7% of the velocity compared to propanoyl-CoA Sus scrofa ADP + phosphate + ?
-
 ?
ATP + crotonyl-CoA + HCO3- at 3% the velocity compared to propanoyl-CoA Sus scrofa ADP + phosphate + ?
-
 ?
ATP + propanoyl-CoA + HCO3-
-
 Sus scrofa ADP + phosphate + methylmalonyl-CoA
-
 ?

Cofactor

Cofactor Comment Organism Structure
biotin 4 mol of biotin bound per mol of enzyme Sus scrofa