Literature summary for 2.1.3.1 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.

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Crystallization (Commentary)

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

Organism

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

Reaction

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

Substrates and Products (Substrate)

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

Subunits

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

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Release 2023.1 (January 2023)