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Titolo:
Xanthine oxidase catalyzes the synthesis of retinoic acid
Autore:
Taibi, G; Paganini, A; Gueli, MC; Ampola, F; Nicotra, CMA;
Indirizzi:
Univ Palermo, Ist Chim Biol, I-90127 Palermo, Italy Univ Palermo PalermoItaly I-90127 Ist Chim Biol, I-90127 Palermo, Italy
Titolo Testata:
JOURNAL OF ENZYME INHIBITION
fascicolo: 3, volume: 16, anno: 2001,
pagine: 275 - 285
SICI:
8755-5093(2001)16:3<275:XOCTSO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALDEHYDE DEHYDROGENASE; BETA-CAROTENE; RAT-LIVER; ALCOHOL-DEHYDROGENASE; ENZYMATIC OXIDATION; 9-CIS-RETINOIC ACID; VITAMIN-A; BIOSYNTHESIS; DIFFERENTIATION; IDENTIFICATION;
Keywords:
retinoic acid; xanthine oxidase; retinaldehyde oxidase; purine inhibition;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Taibi, G Univ Palermo, Ist Chim Biol, I-90127 Palermo, Italy Univ PalermoPalermo Italy I-90127 Biol, I-90127 Palermo, Italy
Citazione:
G. Taibi et al., "Xanthine oxidase catalyzes the synthesis of retinoic acid", J ENZ INHIB, 16(3), 2001, pp. 275-285

Abstract

Milk xanthine oxidase (xanthine: oxygen oxidoreductase; XO; EC 1.1.3.22) was found to catalyze the conversion of retinaldehyde to retinoic acid. The ability of XO to synthesize all trans-retinoic acid efficiently was assessed by its turnover number of 31.56 min(-1), determined at pH 7.0 with 1 nM XO and all trans-retinaldehyde varying between 0.05 to 2 muM. The determination of both retinoid and purine content in milk was also considered in order to correlate their concentrations with kinetic parameters of retinaldehyde oxidase activity. The velocity of the reaction was dependent on the isomeric form of the substrate, the all trans- and 9-cis-forms being the preferred substrates rather than 13-cis-retinaldehyde. The enzyme was able to oxidize retinaldehyde in the presence of oxygen with NAD or without NAD addition. In this latter condition the catalytic efficiency of the enzyme was higher. The synthesis of retinoic acid was inhibited 87% and 54% by 4 muM and 2muM allopurinol respectively and inhibited 48% by 10 muM xanthine in enzyme assays performed at 2 muM all trans-retinaldehyde. The K-i value determined for xanthine as an inhibitor of retinaldehyde oxidase activity was 4 muM.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 06:38:37