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

Jae Hwan Lim; Kwang Yeon Hwang; Juhyun Choi; Duck Yeon Lee; Byung Yoon Ahn; Yunje Cho; Key Sun Kim; Ye Sun Han

doi:10.1006/bbrc.2001.5752

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

Jae Hwan Lim, Kwang Yeon Hwang, Juhyun Choi, Duck Yeon Lee, Byung Yoon Ahn, Yunje Cho, Key Sun Kim, Ye Sun Han

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

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°C. However, the thermostability of the mutant E41A, which has a T_1/2 value of 25 min at 95°C, 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.

Original language	English
Pages (from-to)	263-268
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	288
Issue number	1
DOIs	https://doi.org/10.1006/bbrc.2001.5752
Publication status	Published - 2001 Oct 19

Bibliographical note

Funding Information:
We gratefully acknowledge the financial support from the Korea Institute of Science and Technology and a grant from the Ministry of Science and Technology, Korea.

Keywords

Aquifex pyrophilus
Hydrogen bonds
Ion pair network
Superoxide dismutase
Thermostability

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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

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 T1/2 value of K12A was 210 min and that of the wild type was 175 min at 95°C. However, the thermostability of the mutant E41A, which has a T1/2 value of 25 min at 95°C, 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.",

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AU - Lee, Duck Yeon

AU - Ahn, Byung Yoon

AU - Cho, Yunje

AU - Kim, Key Sun

AU - Han, Ye Sun

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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