Literature summary for 5.4.99.2 extracted from

Kwiecien, R.A.; Khavrutskii, I.V.; Musaev, D.G.; Morokuma, K.; Banerjee, R.; Paneth, P.
Computational insights into the mechanism of radical generation in B12-dependent methylmalonyl-CoA mutase (2006), J. Am. Chem. Soc., 128, 1287-1292.

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Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
(R)-methylmalonyl-CoA = succinyl-CoA	ONIOM calculations based on protein structure. Homolytic Co-C5 bond cleavage in the 5-deoxyadenosylcobalamin cofactor is a stepwise process in which conformational changens in the 5-deoxyadenosine moiety proceed the actual homolysis step. The movement of the deoxyadenosine moity during homolysis positions the resulting 5-deoxyadenosyl radical for the subsequent hydrogen atom transfer from the substrate	Propionibacterium freudenreichii subsp. shermanii	a

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Release 2023.1 (January 2023)