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Titolo:
PROTEIN ENGINEERING REVEALS ANCIENT ADAPTIVE REPLACEMENTS IN ISOCITRATE DEHYDROGENASE
Autore:
DEAN AM; GOLDING GB;
Indirizzi:
FINCH UNIV HLTH SCI CHICAGO MED SCH,DEPT BIOL CHEM N CHICAGO IL 60064 MCMASTER UNIV,DEPT BIOL HAMILTON ON L8S 4K1 CANADA
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 7, volume: 94, anno: 1997,
pagine: 3104 - 3109
SICI:
0027-8424(1997)94:7<3104:PERAAR>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
3-ISOPROPYLMALATE DEHYDROGENASE; THERMUS-THERMOPHILUS; SEQUENCE ALIGNMENT; BRANCH POINT; EVOLUTION; MECHANISM; TRANSHYDROGENASE; PHOSPHORYLATION; SPECIFICITY; NUCLEOTIDE;
Keywords:
ISOPROPYLMALATE DEHYDROGENASE; NAD; NADP; ANCIENT ADAPTATIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
A.M. Dean e G.B. Golding, "PROTEIN ENGINEERING REVEALS ANCIENT ADAPTIVE REPLACEMENTS IN ISOCITRATE DEHYDROGENASE", Proceedings of the National Academy of Sciences of the United Statesof America, 94(7), 1997, pp. 3104-3109

Abstract

Evolutionary analysis indicates that eubacterial NADP-dependent isocitrate dehydrogenases (EC 1.1.1.42) first evolved from an NAD-dependentprecursor about 3.5 billion years ago. Selection in favor of utilizing NADP was probably a result of niche expansion during growth on acetate, where isocitrate dehydrogenase provides 90% of the NADPH necessaryfor biosynthesis. Amino acids responsible for differing coenzyme specificities were identified from x-ray crystallographic structures of Escherichia coli isocitrate dehydrogenase and the distantly related Thermus thermophilus NAD-dependent isopropylmalate dehydrogenase. Site-directed mutagenesis at sites lining the coenzyme binding pockets has been used to invert the coenzyme specificities of both enzymes, Reconstructed ancestral sequences indicate that these replacements are ancestral, Hence the adaptive history of molecular evolution is amenable to experimental investigation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 05:28:01