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Literature summary extracted from

  • Shenoy, B.C.; Magner, W.J.; Kumar, G.K.; Phillips, N.F.B.; Haase, F.C.; Samols, D.
    The nonbiotinylated form of the 1.3 S subunit of transcarboxylase binds to avidin (monomeric)-agarose: Purification and separation from the biotinylated 1.3 S subunit (1993), Protein Expr. Purif., 4, 85-94.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.1 1.3S subunit cloned and expressed in Escherichia coli 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 recombinant enzyme and mutant 1.3S subunit, affinity chromatography on avidin(monomeric)-agarose, copurification of apo and biotinylated 1.3S forms Propionibacterium freudenreichii subsp. shermanii

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.3.1 (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate partial reaction 1 is catalysed specifically by the 12S subunit, partial reaction 2 is catalysed specifically by the 5S subunit Propionibacterium freudenreichii subsp. shermanii
a

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

Subunits

EC Number Subunits Comment Organism
2.1.3.1 More amino acid sequence of biotinyl subunit Propionibacterium freudenreichii subsp. shermanii
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
2.1.3.1 More 1.3 S is homogen, SDS-PAGE Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.1 biotin requirement Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 biotin biotin containing subunit of enzyme acts as a carboxyl carrier between the CoA ester sites on the central 12S subunit of enzyme and keto acid sites on outer 5S subunit of enzyme and links the 12S and 5S subunits together to form a 26S multisubunit enzyme complex, biotin content: 28% Propionibacterium freudenreichii subsp. shermanii