Literature summary for 2.1.3.1 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.

Search for more literature for 2.1.3.1

Cloned(Commentary)

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

Protein Variants

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 [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

Metals/Ions	Comment	Organism	Structure
Co2+	requirement	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	-	-	-

Purification (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
propionyl-CoA + oxaloacetate	-	Propionibacterium freudenreichii subsp. shermanii	(S)-methylmalonyl-CoA + pyruvate	-	r

Subunits

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

Turnover Number [1/s]

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

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

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Release 2023.1 (January 2023)