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Article

Role of proline residues in conferring thermostability on aqualysin I.

Journal of biochemistry - 1 Feb 2007

Sakaguchi Masayoshi, Matsuzaki Mika, Niimiya Keisuke, Seino Junichi, Sugahara Yasusato, Kawakita Masao

Abstract excerpt

To understand the molecular basis of the thermostability of a thermophilic serine protease aqualysin I from Thermus aquaticus YT-1, we introduced mutations at Pro5, Pro7, Pro240 and Pro268, which are located on the surface loops of aqualysin I, by changing these amino acid residues into those found at the corresponding locations in VPR, a psychrophilic serine protease from Vibrio sp. PA-44. All mutants were...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17169970
DOI: 10.1093/jb/mvm025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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