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Titolo:
Mouse alcohol dehydrogenase 4: kinetic mechanism, substrate specificity and simulation of effects of ethanol on retinoid metabolism
Autore:
Plapp, BV; Mitchell, JL; Berst, KB;
Indirizzi:
Univ Iowa, Dept Biochem, Iowa City, IA 52242 USA Univ Iowa Iowa City IA USA 52242 a, Dept Biochem, Iowa City, IA 52242 USA
Titolo Testata:
CHEMICO-BIOLOGICAL INTERACTIONS
fascicolo: 1-3, volume: 130, anno: 2001,
pagine: 445 - 456
SICI:
0009-2797(20010130)130:1-3<445:MAD4KM>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
OMEGA-HYDROXYFATTY ACIDS; POTENTIAL MECHANISM; GENE FAMILY; OXIDATION; INHIBITION; LIVER; EXPRESSION; ALDEHYDES; ISOZYMES;
Keywords:
enzyme kinetics; inhibitors; metabolic simulation; retinoids; substrate specificity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Plapp, BV Univ Iowa, Dept Biochem, Iowa City, IA 52242 USA Univ Iowa IowaCity IA USA 52242 ochem, Iowa City, IA 52242 USA
Citazione:
B.V. Plapp et al., "Mouse alcohol dehydrogenase 4: kinetic mechanism, substrate specificity and simulation of effects of ethanol on retinoid metabolism", CHEM-BIO IN, 130(1-3), 2001, pp. 445-456

Abstract

Mouse ADH4 (purified, recombinant) has a low catalytic efficiency for ethanol and acetaldehyde, but very high activity with longer chain alcohols andaldehydes, at pH 7.3 and temperature 37 degreesC. The observed turnover numbers and catalytic efficiencies for the oxidation of all-trans-retinol andthe reduction of all-trans-retinal and 9-cis-retinal are low relative to other substrates; 9-cis-retinal is more reactive than all-trans-retinal. Thereduction of all-trans- or 9-cis-retinals coupled to the oxidation of ethanol by NAD(+) is as efficient as the reduction with NADH. However, the Michaelis constant for ethanol is about 100 mM, which indicates that the activity would be lower at physiologically relevant concentrations of ethanol, Simulations of the oxidation of retinol to retinoic acid with mouse ADH4 and human aldehyde dehydrogenase (ALDH1), using rate constants estimated for all steps in the mechanism, suggest that ethanol (50 mM) would modestly decrease production of retinoic acid. However, if the K-m for ethanol were smaller, as for human ADH4, the rate of retinol oxidation and formation of retinoic acid would be significantly decreased during metabolism of 50 mM ethanol. These studies begin to describe quantitatively the roles of enzymes involved in the metabolism of alcohols and carbonyl compounds. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 12:41:39