title: A carbon-skeleton walk: a novel double rearrangement of glutaryl-CoA catalyzed by the human methylmalonyl-CoA mutase.
abstract: Methylmalonyl-CoA mutase is a member of the coenzyme B12-dependent family of isomerases and interconverts methylmalonyl-CoA and succinyl-CoA. We have examined the ability of the enzyme to effect a double rearrangement reaction when presented with glutaryl-CoA, a substrate analog with a three-carbon template on which two successive 1,2 migrations can occur. Our results demonstrate that the enzyme converts glutaryl-CoA to both methylsuccinyl-CoA and ethylmalonyl-CoA. To our knowledge, this is the first example of a double rearrangement reaction catalyzed by a coenzyme B12-dependent enzyme.
authors.affiliation: Biochemistry Department, Beadle Center, University of Nebraska, Lincoln 68588-0664, USA.
authors.forename: R
authors.initials: R
authors.lastname: Padmakumar
authors.forename: R
authors.initials: R
authors.lastname: Banerjee
mesh_terms: D000214:Acyl Coenzyme A / Q000737:chemistry*; D002244:Carbon / Q000737:chemistry*; D002384:Catalysis; D006801:Humans; D008765:Methylmalonyl-CoA Mutase / Q000737:chemistry*; D015394:Molecular Structure
chemical_list: D000214:Acyl Coenzyme A; C102829:ethylmalonyl-coenzyme A; C102828:methylsuccinyl-coenzyme A; C015901:glutaryl-coenzyme A; D002244:Carbon; D008765:Methylmalonyl-CoA Mutase