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Literature summary for 2.1.3.1 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)

Cloned (Comment) Organism
1.3S subunit cloned and expressed in Escherichia coli 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
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

Reaction Comment Organism Reaction ID
(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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
biotin requirement Propionibacterium freudenreichii subsp. shermanii
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