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Titolo:
Thermostabilization of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase
Autore:
Numata, K; Hayashi-Iwasaki, Y; Kawaguchi, J; Sakurai, M; Moriyama, H; Tanaka, N; Oshima, T;
Indirizzi:
Tokyo Univ Pharm & Life Sci, Dept Mol Biol, Hachioji, Tokyo 1920392, JapanTokyo Univ Pharm & Life Sci Hachioji Tokyo Japan 1920392 o 1920392, Japan Tokyo Inst Technol, Dept Life Sci, Yokohama, Kanagawa 2268501, Japan TokyoInst Technol Yokohama Kanagawa Japan 2268501 anagawa 2268501, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 1-2, volume: 1545, anno: 2001,
pagine: 174 - 183
SICI:
0167-4838(20010209)1545:1-2<174:TOACEB>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYNTHASE-ALPHA-SUBUNIT; 3-ISOPROPYLMALATE DEHYDROGENASE; EXTREME THERMOPHILE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; PYROCOCCUS-FURIOSUS; NUCLEOTIDE-SEQUENCE; CRYSTAL-STRUCTURES; BACILLUS-SUBTILIS; HYDROPHOBIC CORE; PROLINE RESIDUES;
Keywords:
3-isopropylmalate dehydrogenase; chimera; protein stability; site-directed mutagenesis; Thermus thermophilus;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Oshima, T Tokyo Univ Pharm & Life Sci, Dept Mol Biol, Hachioji, Tokyo 1920392, Japan Tokyo Univ Pharm & Life Sci Hachioji Tokyo Japan 1920392 Japan
Citazione:
K. Numata et al., "Thermostabilization of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase", BBA-PROT ST, 1545(1-2), 2001, pp. 174-183

Abstract

A chimeric 3-isopropylmalate dehydrogenase, named 2T2M6T, made of parts from an extreme thermophile, Thermus thermophilus, and a mesophile, Bavillus subtilis, was found to be considerably more labile than the T. thermophiluswild-type isopropylmalate dehydrogenase. In order to identify the molecular basis of the thermal stability of the T. thermophilus isopropylmalate dehydrogenase, 11 amino acid residues in the mesophilic portion of the chimerawere substituted by the corresponding residues of the T. thermophilus enzyme, and the effects of the side chain substitutions were analyzed by comparing the reaction rate of irreversible heat denaturation and catalytic parameters of the mutant chimeras with those of the original chimera, 2T2M6T. Four single-site mutants were successfully stabilized without any loss of thecatalytic function. All these four sites are located in loop regions of the enzyme. Our results strongly suggest the importance of these loop structures to the extreme stability of the T. thermophilus isopropylmalate dehydrogenase. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 06:42:27