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Titolo:
Characterization of a major form of human isatin reductase and the reducedmetabolite
Autore:
Usami, N; Kitahara, K; Ishikura, S; Nagano, M; Sakai, S; Hara, A;
Indirizzi:
Gifu Pharmaceut Univ, Biochem Lab, Gifu 5028585, Japan Gifu Pharmaceut Univ Gifu Japan 5028585 Biochem Lab, Gifu 5028585, Japan Gifu Prefectural Gifu Hosp, Dept Urol, Gifu, Japan Gifu Prefectural Gifu Hosp Gifu Japan Gifu Hosp, Dept Urol, Gifu, Japan
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 22, volume: 268, anno: 2001,
pagine: 5755 - 5763
SICI:
0014-2956(200111)268:22<5755:COAMFO>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONOAMINE-OXIDASE INHIBITOR; CARBONYL REDUCTASE; DIHYDRODIOL DEHYDROGENASE; TISSUE DISTRIBUTION; HUMAN-LIVER; RAT-BRAIN; EXPRESSION; PURIFICATION; OXIDATION; IDENTITY;
Keywords:
carbonyl reductase; 3-hydroxy-2-oxoindole; isatin; monoamine oxidase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Hara, A Gifu Pharmaceut Univ, Biochem Lab, Gifu 5028585, Japan Gifu Pharmaceut Univ Gifu Japan 5028585 Lab, Gifu 5028585, Japan
Citazione:
N. Usami et al., "Characterization of a major form of human isatin reductase and the reducedmetabolite", EUR J BIOCH, 268(22), 2001, pp. 5755-5763

Abstract

Isatin, an endogenous indole, has been shown to inhibit monoamine oxidase,and exhibit various pharmacological actions. However, the metabolism of isatin in humans remains unknown. We have found high isatin reductase activity in the 105 000 g supernatants of human liver and kidney homogenates, and have purified and characterized a major form of the enzyme in the two tissues. The hepatic and renal enzymes showed the same properties, including an M-r of 31 kDa, substrate specificity for carbonyl compounds and inhibitor sensitivity, which were also identical to those of recombinant human carbonyl reductase. The identity of the isatin reductase with carbonyl reductase was immunologically demonstrated with an antibody against the recombinant carbonyl reductase. About 90% of the soluble isatin reductase activity in theliver and kidney was immunoprecipitated by the antibody. The K-m (10 muM) and k(cat)/K-m (1.7 s(-1) muM(-1)) values for isatin at pH 7.0 were comparable to those for phenanthrenequinone, the best xenobiotic substrate of carbonyl reductase. The reduced product of isatin was chemically identified with 3-hydroxy-2-oxoindole, which is also excreted in human urine. The inhibitory potency of the reduced product for monoamine oxidase A and B was significantly lower than that of isatin. The results indicate that the novel metabolic pathway of isatin in humans is mediated mainly by carbonyl reductase,which may play a critical role in controlling the biological activity of isatin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 19:49:02