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Titolo:
Crystal structures of mutants of Thermus thermophilus IPMDH adapted to lowtemperatures
Autore:
Hirose, R; Suzuki, T; Moriyama, H; Sato, T; Yamagishi, A; Oshima, T; Tanaka, N;
Indirizzi:
Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Life Sci, Midori Ku, Yokohama, Kanagawa 2268501, Japan Tokyo Inst Technol Yokohama Kanagawa Japan 2268501 anagawa 2268501, Japan Tokyo Univ Pharm & Life Sci, Sch Life Sci, Tokyo 1920392, Japan Tokyo UnivPharm & Life Sci Tokyo Japan 1920392 ci, Tokyo 1920392, Japan
Titolo Testata:
PROTEIN ENGINEERING
fascicolo: 2, volume: 14, anno: 2001,
pagine: 81 - 84
SICI:
0269-2139(200102)14:2<81:CSOMOT>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
3-ISOPROPYLMALATE DEHYDROGENASE; COLD ADAPTATION; ISOPROPYLMALATE DEHYDROGENASE; MOLECULAR-REPLACEMENT; EXTREME THERMOPHILE; ESCHERICHIA-COLI; MECHANISM; PROTEINS; THERMOSTABILITY; SPECIFICITY;
Keywords:
cold-adapted mutants; 3-isopropylmalate dehydrogenase; thermal stability; Thermus thermophilus; structural analysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Tanaka, N Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Life Sci,Midori Ku, Nagatsuta 4259, Yokohama, Kanagawa 2268501, Japan Tokyo Inst Technol Nagatsuta 4259 Yokohama Kanagawa Japan 2268501
Citazione:
R. Hirose et al., "Crystal structures of mutants of Thermus thermophilus IPMDH adapted to lowtemperatures", PROTEIN ENG, 14(2), 2001, pp. 81-84

Abstract

Random mutagenesis on thermophilic 3-isopropylmalate dehydrogenases (IPMDH; EC 1.1.1.85) produced mutant enzymes which adapt to low temperatures. These mutants had higher activity at lower temperatures than the wildtype enzyme without losing high thermostability. Here we report three structures of the mutants of Thermus thermophilus IPMDH determined by X-ray diffraction which was adapted to a low-temperature environment. Two of them have unstable coenzyme binding states and the other one probably has a stable substratebinding state. The present research suggests that the adaptation is correlated with the binding of either coenzyme or the substrate.

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Documento generato il 05/12/20 alle ore 19:53:01