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Article

Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria.

The Journal of biological chemistry - 24 Apr 2015

Kobayashi Hidetomo, Yoshida Toru, Miyakawa Takuya, Tashiro Mitsuru, Okamoto Keinosuke, Yamanaka Hiroyasu, Tanokura Masaru, Tsuge Hideaki

Abstract excerpt

Subtilisin-like proteases are broadly expressed in organisms ranging from bacteria to mammals. During maturation of these enzymes, N-terminal propeptides function as intramolecular chaperones, assisting the folding of their catalytic domains. However, we have identified an exceptional case, the serine protease from Aeromonas sobria (ASP), that lacks a propeptide. Instead, ORF2, a protein encoded just downstream...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 25784551
DOI: 10.1074/jbc.M114.622852
PMCID: PMC4409271

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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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