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Article

Mutational effects on thermostable superoxide dismutase from Aquifex pyrophilus: understanding the molecular basis of protein thermostability.

Biochemical and biophysical research communications - 19 Oct 2001

Lim J H, Hwang K Y, Choi J, Lee D Y, Ahn B Y, Cho Y, Kim K S, Han Y S

Abstract excerpt

We designed two mutants of superoxide dismutase (SOD), one is thermostable and the other is thermolabile, which provide valuable insight to identify amino acid residues essential for the thermostability of the SOD from Aquifex pyrophilus (ApSOD). The mutant K12A, in which Lys12 was replaced by Ala, had increased thermostability compared to that of the wild type. The T(1/2) value of K12A was 210 min and that of...

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Identifiers

PMID: 11594783
DOI: 10.1006/bbrc.2001.5752

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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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