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Titolo:
The A245K mutation exposes another stage of the bacterial L-lactate dehydrogenase reaction mechanism
Autore:
Kedzierski, P; Moreton, K; Clarke, AR; Holbrook, JJ;
Indirizzi:
Wroclaw Tech Univ, Inst Phys & Theoret Chem, PL-50370 Wroclaw, Poland Wroclaw Tech Univ Wroclaw Poland PL-50370 Chem, PL-50370 Wroclaw, Poland Univ Bristol, Dept Biochem, Bristol, Avon, England Univ Bristol Bristol Avon England , Dept Biochem, Bristol, Avon, England Univ Bristol, Mol Recognit Ctr, Bristol, Avon, England Univ Bristol Bristol Avon England l Recognit Ctr, Bristol, Avon, England
Titolo Testata:
BIOCHEMISTRY
fascicolo: 24, volume: 40, anno: 2001,
pagine: 7247 - 7252
SICI:
0006-2960(20010619)40:24<7247:TAMEAS>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; BACILLUS-STEAROTHERMOPHILUS; PYRUVATE; INTERCONVERSION; FRAMEWORK; QUANTUM; RESIDUE; ENZYME; STATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Kedzierski, P Wroclaw Tech Univ, Inst Phys & Theoret Chem, PL-50370 Wroclaw, Poland Wroclaw Tech Univ Wroclaw Poland PL-50370 Wroclaw, Poland
Citazione:
P. Kedzierski et al., "The A245K mutation exposes another stage of the bacterial L-lactate dehydrogenase reaction mechanism", BIOCHEM, 40(24), 2001, pp. 7247-7252

Abstract

The A245K mutant of Bacillus stearothermophilus L-lactate dehydrogenase has been expressed in Escherichia coli and purified. A qualitative change in the reaction mechanism prior to the hydride transfer step in the reverse direction in the mutant is revealed. Both transient and steady state characteristics of the mutant are presented and show in contrast to the wild-type enzyme where a rearrangement of an enzyme-NADH-pyruvate complex is rate-limiting that in the mutant the rearrangement is much faster and hydride transfer is the first slow step. The steady state is limited by a new second slower conformation change involving an NAD(+) complex. The mutation may provide a valuable framework for inhibitor and drug design research.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 21:03:01