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dc.contributor.authorSAH, Sen_US
dc.contributor.authorPHALE, PSen_US
dc.date.accessioned2012-06-26T05:23:23Z
dc.date.available2012-06-26T05:23:23Z
dc.date.issued2011en_US
dc.identifier.citationBIODEGRADATION,22(3)517-526en_US
dc.identifier.issn0923-9820en_US
dc.identifier.urihttp://dx.doi.org/10.1007/s10532-010-9424-2en_US
dc.identifier.urihttp://dspace.library.iitb.ac.in/jspui/handle/100/13959
dc.description.abstract1-Naphthol 2-hydroxylase (1-NH) which catalyzes the conversion of 1-naphthol to 1,2-dihydroxynaphthalene was purified to homogeneity from carbaryl-degrading Pseudomonas sp. strain C6. The enzyme was found to be a homodimer with subunit molecular weight of 66 kDa. UV, visible and fluorescence spectral properties, identification of flavin moiety by HPLC as FAD, and reconstitution of apoenzyme by FAD suggest that enzyme is FAD-dependent. 1-NH accepts electron from NADH as well as NADPH. Besides 1-naphthol (K (m), 9.1 mu M), the enzyme also accepts 5-amino 1-naphthol (K (m), 6.4 mu M) and 4-chloro 1-naphthol (K (m), 2.3 mu M) as substrates. Enzyme showed substrate inhibition phenomenon at high concentration of 1-naphthol (K (i), 283 mu M). Stoichiometric consumption of oxygen and NADH, and biochemical properties suggest that 1-NH belongs to FAD containing external flavomonooxygenase group of oxido-reductase class of enzymes. Based on biochemical and kinetic properties, 1-NH from Pseudomonas sp. strain C6 appears to be different than that reported earlier from Pseudomonas sp. strain C4. Chemical modification and protection by 1-naphthol and NADH suggest that His, Arg, Cys, Tyr and Trp are at or near the active site of 1-NH.en_US
dc.language.isoEnglishen_US
dc.publisherSPRINGERen_US
dc.subjectPara-Hydroxybenzoate Hydroxylaseen_US
dc.subjectAdenine-Dinucleotide Phosphateen_US
dc.subjectPhenol Hydroxylaseen_US
dc.subjectCrystal-Structureen_US
dc.subjectCatalytic Cycleen_US
dc.subjectBinding-Siteen_US
dc.subjectCarbarylen_US
dc.subjectFlavinen_US
dc.subjectResidueen_US
dc.subjectEnzymeen_US
dc.subject.otherCarbaryl Metabolismen_US
dc.subject.other1-Naphthol 2-Hydroxylaseen_US
dc.subject.otherFlavoenzymeen_US
dc.subject.otherKinetic Propertiesen_US
dc.subject.otherChemical Modificationen_US
dc.subject.otherActive-Site Residuesen_US
dc.title1-Naphthol 2-hydroxylase from Pseudomonas sp. strain C6: purification, characterization and chemical modification studiesen_US
dc.typeArticleen_US


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