Literature summary extracted from

Zheng, X.; Rivera-Hainaj, R.E.; Zheng, Y.; Pusztai-Carey, M.; Hall, P.R.; Yee, V.C.; Carey, P.R.
Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: raman crystallographic evidence (2002), Biochemistry, 41, 10741-10746.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.1.3.1	Raman spectroscopy	Propionibacterium freudenreichii subsp. shermanii

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.3.1	Propionibacterium freudenreichii subsp. shermanii	-	-	-

Reaction

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

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.1.3.1	butyryl-CoA + oxaloacetate	-	Propionibacterium freudenreichii subsp. shermanii	ethylmalonyl-CoA + pyruvate	-	?
2.1.3.1	propionyl-CoA + oxaloacetate	two partial reactions	Propionibacterium freudenreichii subsp. shermanii	(S)-methylmalonyl-CoA + pyruvate	-	r

Subunits

EC Number	Subunits	Comment	Organism
2.1.3.1	More	structure	Propionibacterium freudenreichii subsp. shermanii
2.1.3.1	More	MW of 12S hexamer: 338000Da	Propionibacterium freudenreichii subsp. shermanii

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Release 2023.1 (January 2023)