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Titolo:
Mutational effects on thermostable superoxide dismutase from Aquifex pyrophilus: Understanding the molecular basis of protein thermostability
Autore:
Lim, JH; Hwang, KY; Choi, JY; Lee, DY; Ahn, BYY; Cho, YJ; Kim, KS; Han, YS;
Indirizzi:
Pohang Univ Sci & Technol, Dept Life Sci, Pohang, South Korea Pohang Univ Sci & Technol Pohang South Korea e Sci, Pohang, South Korea Korea Univ, Dept Genet Engn, Seoul 136701, South Korea Korea Univ Seoul South Korea 136701 enet Engn, Seoul 136701, South Korea Crystal Genomics Inc, Taejon, South Korea Crystal Genomics Inc Taejon South Korea nomics Inc, Taejon, South Korea Korea Inst Sci & Technol, Struct Biol Res Ctr, Seoul, South Korea Korea Inst Sci & Technol Seoul South Korea Res Ctr, Seoul, South Korea
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 288, anno: 2001,
pagine: 263 - 268
SICI:
0006-291X(20011019)288:1<263:MEOTSD>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
HYPERTHERMOPHILIC BACTERIUM; CONFORMATIONAL STABILITY; GLUTAMATE-DEHYDROGENASE; PYROCOCCUS-FURIOSUS; HIGH-TEMPERATURES; CRYSTAL-STRUCTURE; SALT BRIDGES; ION-PAIRS; KEY ROLE; DETERMINANTS;
Keywords:
thermostability; superoxide dismutase; Aquifex pyrophilus; hydrogen bonds; ion pair network;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Han, YS 39-1 Hawallkok Dong,Sungbuk Ku, Seoul 130650, South Korea 39-1 Hawallkok Dong,Sungbuk Ku Seoul South Korea 130650 th Korea
Citazione:
J.H. Lim et al., "Mutational effects on thermostable superoxide dismutase from Aquifex pyrophilus: Understanding the molecular basis of protein thermostability", BIOC BIOP R, 288(1), 2001, pp. 263-268

Abstract

We designed two mutants of superoxide dismutase (SOD), one is thermostableand 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-1/2value 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

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 01:19:02