Literature summary for 2.1.3.1 extracted from

O'Keefe, S.J.; Knowles, J.R.
Biotin-dependent carboxylation catalyzed by transcarboxylase is a stepwise process [published erratum appears in Biochemistry 1987 Sep 8;26(18):5952] (1986), Biochemistry, 25, 6077-6084.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetic deuterium and 13C-isotope effects	Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	requirement	Propionibacterium freudenreichii subsp. shermanii

Organism

Organism	UniProt	Comment	Textmining
Propionibacterium freudenreichii subsp. shermanii	-	i.e. Propionibacterium freudenreichii	-

Reaction

Reaction	Comment	Organism	Reaction ID
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate	mechanism	Propionibacterium freudenreichii subsp. shermanii	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
17	-	-	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

Temperature Optimum [°C]

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

Cofactor

Cofactor	Comment	Organism	Structure
biotin	requirement	Propionibacterium freudenreichii subsp. shermanii

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Release 2023.1 (January 2023)