The Peptidyl-Prolyl Isomerase Activity of SlyD Is Not Required for Maturation of Escherichia coli Hydrogenase | Zendy

Jie Wei Zhang | Zendy; Michael R. Leach | Zendy; Deborah B. Zamble | Zendy

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The Peptidyl-Prolyl Isomerase Activity of SlyD Is Not Required for Maturation of Escherichia coli Hydrogenase

Author(s) -

Jie Wei Zhang,

Michael R. Leach,

Deborah B. Zamble

Publication year - 2007

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.00922-07

Subject(s) - biology , prolyl isomerase , escherichia coli , isomerase , peptidylprolyl isomerase , hydrogenase , biochemistry , escherichia coli proteins , genetics , pin1 , enzyme , gene

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.

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