Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.3.1 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)

Cloned (Comment) Organism
1.3S subunit cloned and expressed in Escherichia coli Propionibacterium freudenreichii subsp. shermanii

Protein Variants

Protein Variants Comment Organism
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
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]

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
-
-
-

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 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

Cofactor Comment Organism Structure
biotin requirement Propionibacterium freudenreichii subsp. shermanii
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