The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase

J Bacteriol. 2007 Nov;189(21):7942-4. doi: 10.1128/JB.00922-07. Epub 2007 Aug 24.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism*
  • Genetic Variation
  • Kinetics
  • Mutation*
  • Peptidylprolyl Isomerase / genetics
  • Peptidylprolyl Isomerase / metabolism*

Substances

  • Escherichia coli Proteins
  • SlyD protein, E coli
  • Peptidylprolyl Isomerase