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Literature summary extracted from

  • Shenoy, B.C.; Samols, D.; Kumar, G.K.
    The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity (1993), Arch. Biochem. Biophys., 304, 359-366.
    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

Protein Variants

EC Number Protein Variants Comment Organism
2.1.3.1 M88L partial reaction 1: 99% loss activity, partial reaction 2: 65% loss of activity, possibly alterations in the microenvironment of the biocytin Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 M90L partial reaction 1: 50% loss of activity, partial reaction 2: 115% activity compared to the 1.3 wild-type enzyme 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
-
-
-

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

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 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

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.1 biotin requirement Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 biotin covalently linked to the 1.3 subunit to the epsilon-amino group of Lys-89, which lies in the conserved sequence Ala-Met-Lys-Met Propionibacterium freudenreichii subsp. shermanii