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Literature summary extracted from

  • Shenoy, B.C.; Xie, Y.; Park, V.L.; Kumar, G.K.; Beegen, H.; Wood, H.G.; Samols, D.
    The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis (1992), J. Biol. Chem., 267, 18407-18412.
    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 A87G Km not significantly changed, significantly reduced kcat Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 M88A Km not significantly changed, significantly reduced kcat Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 M88C Km not significantly changed, significantly reduced kcat Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 M88L Km not significantly changed, significantly reduced kcat Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 M88T Km not significantly changed, significantly reduced kcat Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 M90L Km and kcat not significantly changed Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 additional information double mutant A87M and M88A Propionibacterium freudenreichii subsp. shermanii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.1 additional information
-
 additional information kinetic parameters of wild-type and mutant enzyme Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 0.0044
-
 pyruvate 5S-subunit Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 0.0077
-
 (2S)-methylmalonyl-coenzyme A
-
 Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.3.1 Co2+ requirement 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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.1 recombinant enzyme and mutant 1.3S subunit Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 separation of transcarboxylase complexes from uncombined 12S, 5S and 1.3S subunits by gel filtration Propionibacterium freudenreichii subsp. shermanii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.1 additional information
-
 comparison of wild-type and mutant enzymes 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
-
 Propionibacterium freudenreichii subsp. shermanii (S)-methylmalonyl-CoA + pyruvate
-
 r

Subunits

EC Number Subunits Comment Organism
2.1.3.1 More amino acid sequence of biotinyl subunit Propionibacterium freudenreichii subsp. shermanii
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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.1 25
-
 assay at Propionibacterium freudenreichii subsp. shermanii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.3.1 additional information
-
 additional information 2530 nmol oxaloacetate per nmol biotin per min Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
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