Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: KEGG:D02011 (FAD)
 5,530 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The effects of various inhibitors and activators on the azo- and nitro-reductases of Moniezia expansa have been studied. Both reductions were partially inhibited by FAD, FMN, riboflavin, allopurinol, dicoumarol, 5-nitro-2-furaldehyde, azide and cyanide at 1 mM. Both reactions were stimulated by hypoxanthine. Menadione, nitrofurantoin, SKF 525-A (2-diethylaminoethyl 2,2-diphenylvalerate) and fluoride were without effect. 2. Xanthine- and aldehyde-oxidase activities were not detected in the enzyme preparation. 3. The substrate specificity of the azo- and nitro-reductases were determined. Azobenzene, 4-dimethylamino-azobenzene and 1,2-dimethyl-4-(4-carboxyphenylazo)-5-hydroxybenzene, nitrobenzene, 4-nitrohippuric acid and the isomers of nitrophenol, nitroanisole, nitrobenzoic acid, nitrobenzaldehyde and nitrobenzyl alcohol were reduced. Nitrobenzaldehyde isomers were not reduced to the alcohols and the coumaric acids were not reduced to the phenylpropionic acids. 4. The products of azo- and nitro-reduction were the corresponding amines; hydroxylamino- and hydrazo-compounds were not detected. 5. The pH optima and cofactor requirements were the same for both azo- and nitro-reduction. Neither reaction was inhibited by oxygen.
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PMID:Azo- and nitro-reductases of the cestode Moniezia expansa. Substrate specificity, reaction products and the effects of flavins and other compounds. 1 14

1. The effects of inhibitors and activators on the azo- and nitro-reductases of Ascaris lumbricoides var suum have been investigated. Both types of reduction were inhibited by FAD, FMN, riboflavin, allopurinol, dicoumarol, 5-nitro-2-furaldehyde, azide and cyanide at concentrations of 1 mM. Neither reaction was inhibited by menadione, nitrofurantoin, SKF 525-A or fluoride. Both reactions were stimulated by addition of hypoxanthine. 2. The enzyme preparation contained no detectable aldehyde oxidase or xanthine oxidase activity. 3. The differences in the effects of flavins and inhibitors on mammalian and nematode azo- and nitro-reductases might have practical significance in the development of anthelmintic synergists.
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PMID:The effect of flavins and enzyme inhibitors on 4-nitrobenzoic acid reductase and azo reductase of Ascaris lumbricoides var suum. 5 46

A ketone monooxygenase was purified from cells of Pseudomonas cepacia grown on 2-tridecanone as sole carbon source. Enzyme stability is maintained by the addition of ethanol, EDTA, and dithiothreitol. Stoichiometric studies show that for 1 mol of undecyl acetate formed, 1 mol of O2 is consumed and 1 mol of NADPH is oxidized. The monooxygenase, purified to homogeneity, has a molecular weight of approximately 123,000 and consists of two equal subunits with molecular weights of 55,000. The enzyme contains FAD and exhibits absorption maxima at 375 and 488 nm. Enzyme activity is inhibited by thiol-active reagents and the inhibition by the cations, cadmium, copper, zinc, and mercury, is reversed by dithiothreitol, indicating the presence of essential sulfhydryl groups. Substrate specificity tests show that acetate esters are formed from methyl ketones from C-7 through C-14. The oxygenase is also active on isomers of 2-tridecanone forming esters from 3- through 7-tridecanone. With 6-tridecanone, two esters are formed, heptyl hexanoate and pentyl octanoate, indicating that oxygen is inserted on either side of the carbonyl group. In addition, the enzyme catalyzes the lactonization of the cyclic ketone, cyclopentanone, with the formation of 5-valerolactone.
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PMID:A novel ketone monooxygenase from Pseudomonas cepacia. Purification and properties. 92 12