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Article

Functional similarities of a thermostable protein-disulfide oxidoreductase identified in the archaeon Pyrococcus horikoshii to bacterial DsbA enzymes.

Extremophiles : life under extreme conditions - 1 Jan 2007

Kuroita Toshihiro, Kanno Takuya, Kawai Atsushi, Kawakami Bunsei, Oka Masanori, Endo Yaeta, Tozawa Yuzuru

Abstract excerpt

We have isolated and characterized a gene for a putative protein-disulfide oxidoreductase (phdsb) in the archaeon Pyrococcus horikoshii. The open reading frame of phdsb encodes a protein of 170 amino acids with an NH(2)-terminal extension similar to the bacterial signal peptides. The putative mature region of PhDsb includes a sequence motif, Cys-Pro-His-Cys (CPHC), that is conserved in members of the bacterial...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 16896527
DOI: 10.1007/s00792-006-0015-4

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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