Literature summary for 5.1.99.1 extracted from

Leadlay, P.F.; Fuller, J.Q.
Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii (1983), Biochem. J., 213, 635-642.

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Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA	two enzyme bases are involved in catalysis. One base removes the proton from the substrate, the second provides the new proton. There is no fast isotopic exchange between enzyme-bound intermediates and solvent protons	Propionibacterium freudenreichii subsp. shermanii	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-2-Methyl-3-oxopropanoyl-CoA	-	Propionibacterium freudenreichii subsp. shermanii	(S)-2-Methyl-3-oxopropanoyl-CoA	-	?

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Release 2023.1 (January 2023)