spacer Crystal Structure of Native Methylmalonyl-CoA Epimerase
Primary citation
Title Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold.
Authors McCarthy, A.A.search; Baker, H.M.search; Shewry, S.C.search; Patchett, M.L.search; Baker, E.N.search
Journal STRUCTUREsearch vol:9, pag:637-646 (2001), Identifiers: PubMed ID (11470438)search DOI (10.1016/S0969-2126(01)00622-0)
Abstract Methylmalonyl-CoA epimerase (MMCE) is an essential enzyme in the breakdown of odd-numbered fatty acids and of the amino acids valine, isoleucine, and methionine. Present in many bacteria and in animals, it catalyzes the conversion of (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, the substrate for the B12-dependent enzyme, methylmalonyl-CoA mutase. Defects in this pathway can result in severe acidosis and cause damage to the central nervous system in humans.
MeSH terms Binding Sitessearch, Catalytic Domainsearch, Crystallographysearch, X-Raysearch, Dimerizationsearch, Enzyme Stabilitysearch, Evolutionsearch, Molecularsearch, Metalssearch, Modelssearch, Molecularsearch, Propionibacteriumsearch, Protein Conformationsearch, Racemases and Epimerasessearch
Other entries described in this publication 1jc4
Secondary citations
Title Expression, Crystallization and Preliminary Characterization of Methylmalonyl Coenzyme A Epimerase from Propionibacterium shermanii
Authors Mc Carthy, A.A.search; Baker, H.M.search; Shewry, S.C.search; Kagawa, T.F.search; Saafi, E.search; Patchett, M.L.search; Baker, E.N.search
Journal ACTA CRYSTALLOGR.,SECT.Dsearch vol:57, pag:706-708 (2001) DOI (10.1107/S0907444901002050)
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