Cloned (Comment) | Organism |
---|---|
1.3S subunit cloned and expressed in Escherichia coli | Propionibacterium freudenreichii subsp. shermanii |
Protein Variants | Comment | Organism |
---|---|---|
A87G | Km not significantly changed, significantly reduced kcat | Propionibacterium freudenreichii subsp. shermanii |
M88A | Km not significantly changed, significantly reduced kcat | Propionibacterium freudenreichii subsp. shermanii |
M88C | Km not significantly changed, significantly reduced kcat | Propionibacterium freudenreichii subsp. shermanii |
M88L | Km not significantly changed, significantly reduced kcat | Propionibacterium freudenreichii subsp. shermanii |
M88T | Km not significantly changed, significantly reduced kcat | Propionibacterium freudenreichii subsp. shermanii |
M90L | Km and kcat not significantly changed | Propionibacterium freudenreichii subsp. shermanii |
additional information | double mutant A87M and M88A | Propionibacterium freudenreichii subsp. shermanii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic parameters of wild-type and mutant enzyme | Propionibacterium freudenreichii subsp. shermanii | |
0.0044 | - |
pyruvate | 5S-subunit | Propionibacterium freudenreichii subsp. shermanii | |
0.0077 | - |
(2S)-methylmalonyl-coenzyme A | - |
Propionibacterium freudenreichii subsp. shermanii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | requirement | Propionibacterium freudenreichii subsp. shermanii |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Propionibacterium freudenreichii subsp. shermanii | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme and mutant 1.3S subunit | Propionibacterium freudenreichii subsp. shermanii |
separation of transcarboxylase complexes from uncombined 12S, 5S and 1.3S subunits by gel filtration | Propionibacterium freudenreichii subsp. shermanii |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
comparison of wild-type and mutant enzymes | Propionibacterium freudenreichii subsp. shermanii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
propionyl-CoA + oxaloacetate | - |
Propionibacterium freudenreichii subsp. shermanii | (S)-methylmalonyl-CoA + pyruvate | - |
r |
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 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Propionibacterium freudenreichii subsp. shermanii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | 2530 nmol oxaloacetate per nmol biotin per min | Propionibacterium freudenreichii subsp. shermanii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 |