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

Authors
Lim, JHHwang, KYChoi, JYLee, DYAhn, BYYCho, YJKim, KSHan, YS
Issue Date
2001-10
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.288, no.1, pp.263 - 268
Abstract
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 the wild type was 175 min at 95 degreesC. However, the thermostability of the mutant E41A, which has a T-1/2 value of 25 min at 95 degreesC, was significantly decreased compared to the wild type of ApSOD. To explain the enhanced thermostability of K12A and thermolabile E41A on the structural basis, the crystal structures of the two SOD mutants have been determined. The results have clearly shown the general significance of hydrogen bonds and ion-pair network in the thermostability of proteins. (C) 2001 Academic Press
Keywords
CONFORMATIONAL STABILITY; GLUTAMATE-DEHYDROGENASE; CRYSTAL-STRUCTURE; SALT BRIDGES; ION-PAIRS; KEY ROLE; DETERMINANTS; ENZYME; FORCES; thermostability; superoxide dismutase; Aquifex pyrophilus; hydrogen bonds; ion pair network
ISSN
0006-291X
URI
https://pubs.kist.re.kr/handle/201004/140157
DOI
10.1006/bbrc.2001.5752
Appears in Collections:
KIST Article > 2001
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