Literature summary for 2.1.3.1 extracted from

Hall, P.R.; Zheng, R.; Antony, L.; Pusztai-Carey, M.; Carey, P.R.; Yee, V.C.
Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit (2004), EMBO J., 23, 3621-3631.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
of 5S metalloenzyme subunit, free and in complex with substrate pyruvate, product oxaloacetate, or inhibitor 2-ketobutyrate. Dimer of beta8alpha8 barrels with active site cobalt ion	Propionibacterium freudenreichii subsp. shermanii

Organism

Organism	UniProt	Comment	Textmining
Propionibacterium freudenreichii subsp. shermanii	Q70AC7	5S metalloenzyme subunit	-

Reaction

Reaction	Comment	Organism	Reaction ID
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate	homology model of human pyruvate carboxyltransferase, conserved mechanism	Propionibacterium freudenreichii subsp. shermanii	a

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Propionibacterium freudenreichii subsp. shermanii

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Release 2023.1 (January 2023)