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Titolo:
REDESIGNING SECONDARY STRUCTURE TO INVERT COENZYME SPECIFICITY IN ISOPROPYLMALATE DEHYDROGENASE
Autore:
CHEN RD; GREER A; DEAN AM;
Indirizzi:
FINCH UNIV HLTH SCI CHICAGO MED SCH,DEPT BIOL CHEM N CHICAGO IL 60064
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 22, volume: 93, anno: 1996,
pagine: 12171 - 12176
SICI:
0027-8424(1996)93:22<12171:RSSTIC>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
THERMUS-THERMOPHILUS HB8; ISOCITRATE DEHYDROGENASE; 3-ISOPROPYLMALATE DEHYDROGENASE; EXTREME THERMOPHILE; NUCLEOTIDE-SEQUENCE; MOLECULAR-CLONING; KINETIC MECHANISM; GENE-PRODUCT; PURIFICATION; ENZYME;
Keywords:
PROTEIN ENGINEERING; SPECIFICITY; NAD; NADP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
R.D. Chen et al., "REDESIGNING SECONDARY STRUCTURE TO INVERT COENZYME SPECIFICITY IN ISOPROPYLMALATE DEHYDROGENASE", Proceedings of the National Academy of Sciences of the United Statesof America, 93(22), 1996, pp. 12171-12176

Abstract

Rational engineering of enzymes involves introducing key amino acids guided by a knowledge of protein structure to effect a desirable change in function, To date, all successful attempts to change specificity have been limited to substituting individual amino acids within a protein fold. However, the infant field of protein engineering will only reach maturity when changes in function can be generated by rationally engineering secondary structures, Guided by x-ray crystal structures and molecular modeling, site-directed mutagenesis has been used to systematically invert the coenzyme specificity of Thermus thermophilus isopropylmalate dehydrogenase from a 100-fold preference for NAD to a 1000-fold preference for NADP, The engineered mutant, which is twice as active as wild type, contains four amino acid substitutions and an cy-helix and loop that replaces the original beta-turn, These results demonstrate that rational engineering of secondary structures to produce enzymes with novel properties is feasible.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 14:48:01