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.
D000214:Acyl Coenzyme A / Q000031:analogs & derivatives* / Q000378:metabolism; D001710:Biotin / Q000494:pharmacology; D002262:Carboxy-Lyases / Q000378:metabolism; D002384:Catalysis; D003653:Decarboxylation; D008316:Malonyl Coenzyme A / Q000031:analogs & derivatives* / Q000378:metabolism; D043586:Methylmalonyl-CoA Decarboxylase; D014678:Veillonella / Q000201:enzymology
D000214:Acyl Coenzyme A; C015357:methylmalonyl-coenzyme A; C009061:propionyl-coenzyme A; D008316:Malonyl Coenzyme A; D001710:Biotin; D002262:Carboxy-Lyases; D043586:Methylmalonyl-CoA Decarboxylase