title: Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues.
abstract: Adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii contains no intramolecular disulphide bridges, but two of the six thiol groups in the heterodimer are only revealed after reduction of the denatured enzyme with dithiothreitol. The available evidence suggests that they are present in disulphide linkages to unknown thiols of low Mr. The two specifically masked cysteine residues are Cys-535 in the alpha-subunit and Cys-517 in the beta-subunit, which occupy exactly homologous positions in each chain.
authors.affiliation: Department of Biochemistry, University of Cambridge, U.K.
authors.forename: E N
authors.initials: EN
authors.lastname: Marsh
authors.forename: P F
authors.initials: PF
authors.lastname: Leadlay
mesh_terms: D000595:Amino Acid Sequence; D003545:Cysteine / Q000302:isolation & purification*; D007535:Isomerases / Q000302:isolation & purification*; D008765:Methylmalonyl-CoA Mutase / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D011424:Propionibacterium / Q000201:enzymology*
chemical_list: D007535:Isomerases; D008765:Methylmalonyl-CoA Mutase; D003545:Cysteine