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.
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 |
|