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Article

A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway.

The Journal of biological chemistry - 11 Feb 2005

Zhang Jie Wei, Butland Gareth, Greenblatt Jack F, Emili Andrew, Zamble Deborah B

Abstract excerpt

The [NiFe] centers at the active sites of the Escherichia coli hydrogenase enzymes are assembled by a team of accessory proteins that includes the products of the hyp genes. To determine whether any other proteins are involved in this process, the sequential peptide affinity system was used. The analysis of the proteins in a complex with HypB revealed the peptidyl-prolyl cis/trans-isomerase SlyD, a metal-binding...

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Identifiers

PMID: 15569666
DOI: 10.1074/jbc.M411799200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway.PMID 15569666Read ↗

The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD.Semantic proximity Read ↗

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Maturation of the [NiFe] hydrogenases.Semantic proximity Read ↗

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