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Literature summary for 2.1.3.1 extracted from

  • Berger, M.; Wood, H.G.
    Purification of the subunits of transcarboxylase by affinity chromatography on avidin-sepharose (1975), J. Biol. Chem., 250, 927-933.
    View publication on PubMed

General Stability

General Stability Organism
alkaline pH, low ionic strength, monovalent ions, low protein concentration and elevated temperatures favor dissociation to inactive 5S, 6S and 1.3S subunits Propionibacterium freudenreichii subsp. shermanii

Inhibitors

Inhibitors Comment Organism Structure
Guanidinium chloride Co2+ protects Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000 Propionibacterium freudenreichii subsp. shermanii

Organism

Organism UniProt Comment Textmining
Propionibacterium freudenreichii subsp. shermanii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Propionibacterium freudenreichii subsp. shermanii
affinity chromatography on avidin-Sepharose Propionibacterium freudenreichii subsp. shermanii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.077
-
-
Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii malonyl-CoA + pyruvate
-
?
propionyl-CoA + oxaloacetate
-
Propionibacterium freudenreichii subsp. shermanii (S)-methylmalonyl-CoA + pyruvate
-
r

Subunits

Subunits Comment Organism
More the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000 Propionibacterium freudenreichii subsp. shermanii

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5
-
stable, at pH 8 enzyme dissociates Propionibacterium freudenreichii subsp. shermanii

Cofactor

Cofactor Comment Organism Structure
biotin requirement Propionibacterium freudenreichii subsp. shermanii