title: The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase.
abstract: Escherichia coli SlyD, which is involved in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, exhibits several activities including that of a peptidyl-prolyl isomerase (PPIase). Mutations that result in deficient PPIase activity do not produce corresponding decreases in the other activities of SlyD in vitro or in hydrogenase production levels in vivo.
authors.affiliation: Department of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6.
authors.forename: Jie Wei
authors.initials: JW
authors.lastname: Zhang
authors.forename: Michael R
authors.initials: MR
authors.lastname: Leach
authors.forename: Deborah B
authors.initials: DB
authors.lastname: Zamble
mesh_terms: D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000235:genetics* / Q000378:metabolism*; D014644:Genetic Variation; D007700:Kinetics; D009154:Mutation; D019696:Peptidylprolyl Isomerase / Q000235:genetics / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; C085606:SlyD protein, E coli; D019696:Peptidylprolyl Isomerase