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Literature summary extracted from

  • O'Keefe, S.J.; Knowles, J.R.
    Biotin-dependent carboxylation catalyzed by transcarboxylase is a stepwise process [published erratum appears in Biochemistry 1987 Sep 8;26(18):5952] (1986), Biochemistry, 25, 6077-6084.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.1 additional information
-
additional information kinetic deuterium and 13C-isotope effects Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.3.1 Co2+ requirement Propionibacterium freudenreichii subsp. shermanii

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.1 Propionibacterium freudenreichii subsp. shermanii
-
i.e. Propionibacterium freudenreichii
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.3.1 (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate mechanism Propionibacterium freudenreichii subsp. shermanii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.1 17
-
-
Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.1 propionyl-CoA + oxaloacetate two partial reactions Propionibacterium freudenreichii subsp. shermanii (S)-methylmalonyl-CoA + pyruvate
-
r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.1 30
-
assay at Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.1 biotin requirement Propionibacterium freudenreichii subsp. shermanii