Stereochemistry of the methylmalonyl-CoA decarboxylation reaction.
The steric course of the decarboxylation of (S)-methylmalonyl-CoA to propionyl-CoA, catalyzed by the biotin-dependent sodium pump methylmalonyl-CoA decarboxylase of Veillonella alcalescens was determined. The decarboxylation of (S)-methylmalonyl-CoA in 3H2O yielded (R)-[2-3H]propionyl-CoA; and the decarboxylation of (S)-[2-3H]methylmalonyl-CoA in H2O produced (S)-[2-3H]propionyl-CoA. The results demonstrate retention of configuration during the decarboxylation reaction. The substrate stereochemistry of methylmalonyl-CoA decarboxylase is thus the same as that of all other biotin-containing enzymes investigated.[1]References
- Stereochemistry of the methylmalonyl-CoA decarboxylation reaction. Hoffmann, A., Dimroth, P. FEBS Lett. (1987) [Pubmed]
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