Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The initial reactions in the oxidation of naphthalene by Pseudomonas sp. strain NCIB 9816 involves the enzymatic incorporation of one molecule of oxygen into the aromatic nucleus to form (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The enzyme catalyzing this reaction, naphthalene dioxygenase, was resolved into three protein components, designated A, B, and C, by DEAE-cellulose chromatography. Incubation of naphthalene with components A, B, and C in the presence of NADH resulted in the formation of (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The ratio of oxygen and NADH utilization to product formation was 1:1:1. NADPH also served as an electron donor for naphthalene oxygenation. However, its activity was less than 50% of that observed with NADH. Component A showed NAD(P)H-cytochrome c reductase activity which was stimulated by the addition of flavin adenine dinucleotide and flavin mononucleotide. A similar stimulation was observed when these flavin nucleotides were added to the naphthalene dioxygenase assay system. These preliminary observations indicate that naphthalene dioxygenase has properties in common with both monooxygenase and dioxygenase multicomponent enzyme systems.
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PMID:Oxidation of naphthalene by a multicomponent enzyme system from Pseudomonas sp. strain NCIB 9816. 703 44

Five yeast species, namely Candida tropicalis, Cryptococcus laurentii, Trichosporon asahii, Rhodotorula mucilaginosa and Candida rugosa isolated from hydrocarbon-contaminated soil were found to be potent degraders of diesel oil. These microorganisms showed the presence of enzymes cytochrome P450, NADPH cytochrome c reductase, aminopyrine N demethylase, alcohol dehydrogenase, aldehyde dehydrogenase, naphthalene dioxygenase, catalase and glutathione S transferase when the cells were incubated for 48 h in Bushnell Haas medium supplemented with 2% diesel oil as the sole source of carbon. The cytochrome P450 monooxygenase enzyme system was found to play an important role in diesel oil degradation. A plasmid approximately 12kb in size was found to be harboured by all the yeast species. The role of the plasmid on diesel oil degradation was assessed by biomass inhibition studies, which confirmed that the metabolic machinery of yeast species for diesel oil degradation was plasmid coded. This is the first report establishing the involvement of a plasmid in diesel oil degradation by yeast species.
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PMID:Role of plasmid in diesel oil degradation by yeast species isolated from petroleum hydrocarbon-contaminated soil. 2262 39