Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
USE OF COMPETITIVE DEAD-END INHIBITORS TO DETERMINE THE CHEMICAL MECHANISM OF ACTION OF YEAST ALCOHOL-DEHYDROGENASE
Autore:
LESKOVAC V; TRIVIC S; ANDERSON BM;
Indirizzi:
UNIV NOVI SAD,FAC TECHNOL,BULEVAR CARA LAZARA 1 YU-21000 NOVI SAD YUGOSLAVIA FAC SCI NOVI SAD NOVI SAD YUGOSLAVIA VIRGINIA POLYTECH INST & STATE UNIV BLACKSBURG VA 24061
Titolo Testata:
Molecular and cellular biochemistry
fascicolo: 1-2, volume: 178, anno: 1998,
pagine: 219 - 227
SICI:
0300-8177(1998)178:1-2<219:UOCDIT>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRIMARY ALIPHATIC-ALCOHOLS; TERNARY COMPLEXES; SITE; HISTIDINE; SUBSTRATE; PH; PARAMETERS; ALDEHYDES; RESIDUE; ENZYME;
Keywords:
YEAST ALCOHOL DEHYDROGENASE; DEAD-END INHIBITORS; MECHANISM OF ACTION OF DEHYDROGENASES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
V. Leskovac et al., "USE OF COMPETITIVE DEAD-END INHIBITORS TO DETERMINE THE CHEMICAL MECHANISM OF ACTION OF YEAST ALCOHOL-DEHYDROGENASE", Molecular and cellular biochemistry, 178(1-2), 1998, pp. 219-227

Abstract

In this work, we have postulated a comprehensive and unified chemicalmechanism of action for yeast alcohol dehydrogenase (EC 1.1.1.1, constitutive, cytoplasmic), isolated from Saccharomyces cerevisiae. The chemical mechanism of yeast enzyme is based on the integrity of the proton relay system: His-51....NAD(+)....Thr-48....R.CH2OH(H2O)....Zn++ stretching from His-51 on the surface of enzyme to the active site zinc atom in the substrate-binding site of enzyme. Further, it is based on extensive studies of steady-state kinetic properties of enzyme which were published recently. In this study, we have reported the pH-dependence of dissociation constants for several competitive dead-end inhibitors of yeast enzyme from their binary complexes with enzyme, or their ternary complexes with enzyme and NAD(+) or NADH; inhibitors include: pyrazole, acetamide, sodium azide, 2-fluoroethanol, and 2,2,2-trifluorethanol. The unified mechanism describes the structures of four dissociation forms of apoenzyme, two forms of the binary complex E.NAD(+), three forms of the ternary complex E.NAD(+).alcohol, two forms of the ternary complex E.NADH.aldehyde and three binary complexes E.NADH. Appropriate pK(a) values have been ascribed to protonation forms of most of the above mentioned complexes of yeast enzyme with coenzymes and substrates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:32:47