Literature summary for 5.4.99.2 extracted from

Gaudemer, A.; Zylber, J.; Zylber, N.; Baran-Marszac, M.; Hull, W.E.; Fountoulakis, M.; K�nig, A.; W�lfle, K.; Retey, J.
Reversible cleavage of the cobalt-carbon bond of coenzyme B12 catalyzed by methylmalonyl-CoA mutase from Propionibacterium shermanii. The use of coenzyme B12 stereospecifically deuterated in position 5' (1981), Eur. J. Biochem., 119, 279-285.

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Organism

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-2-methylmalonyl-CoA	-	Propionibacterium freudenreichii subsp. shermanii	succinyl-CoA	-	?

Cofactor

Cofactor	Comment	Organism	Structure
cobamide	enzyme-bound and free 5'-deoxyadenonosylcobalamin molecules are frequently exchanged during incubation, deuterium is transferred from the 5' position of 5'-deoxyadenonosylcobalamin to the solvent, deuterium scrambling between the two diastereotopic 5'-positions occurrs	Propionibacterium freudenreichii subsp. shermanii

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Release 2023.1 (January 2023)