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Titolo:
Comparison of the chemical mechanisms of action of yeast and equine liver alcohol dehydrogenase
Autore:
Leskovac, V; Trivic, S; Anderson, BM;
Indirizzi:
Fac Technol, YU-21000 Novi Sad, Yugoslavia Fac Technol Novi Sad Yugoslavia YU-21000 , YU-21000 Novi Sad, Yugoslavia Fac Sci, Novi Sad, Yugoslavia Fac Sci Novi Sad YugoslaviaFac Sci, Novi Sad, Yugoslavia Virginia Polytech Inst & State Univ, Blacksburg, VA 24061 USA Virginia Polytech Inst & State Univ Blacksburg VA USA 24061 VA 24061 USA
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 3, volume: 264, anno: 1999,
pagine: 840 - 847
SICI:
0014-2956(199909)264:3<840:COTCMO>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRIMARY ALIPHATIC-ALCOHOLS; KINETIC MECHANISM; PH; BINDING; CATALYSIS; ALDEHYDES;
Keywords:
chemical mechanism of action; yeast alcohol dehydrogenase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Leskovac, V Fac Technol, Bulevar Cara Lazara 1, YU-21000 Novi Sad, Yugoslavia Fac Technol Bulevar Cara Lazara 1 Novi Sad Yugoslavia YU-21000
Citazione:
V. Leskovac et al., "Comparison of the chemical mechanisms of action of yeast and equine liver alcohol dehydrogenase", EUR J BIOCH, 264(3), 1999, pp. 840-847

Abstract

The pH-dependence of the steady-state kinetic parameters and the ligand-binding parameters for competitive dead-end inhibitors for the yeast alcohol dehydrogenase (EC 1.1.1.1, constitutive, cytoplasmic) reaction was studied in the pH range 6-10. These studies were designed in order to assign the appropriate pK(a), values to all dissociation forms of enzyme in the chemicalmechanism of action for the yeast enzyme, previously proposed by Cook and Cleland [P.F Cook & W. W. Cleland (1981) Biochemistry 20, 1796-1816]. Tn addition, the chemical mechanism of action for the yeast enzyme, proposed in this work, was compared with a similar mechanism of action for the horse liver enzyme, proposed by Cook and Cleland. Substantial differences were found, especially in the binding of coenzymes and in the structure of enzyme-coenzyme complexes.

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Documento generato il 19/09/20 alle ore 07:14:45