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Literature summary 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

EC Number General Stability Organism
2.1.3.1 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

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.1 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

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.1
-
 Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 affinity chromatography on avidin-Sepharose 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 0.077
-
-
 Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.1.3.1 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

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.3.1 6.5
-
 stable, at pH 8 enzyme dissociates Propionibacterium freudenreichii subsp. shermanii

Cofactor

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