Structural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase

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dc.contributor.authorMyung Hee Kim-
dc.contributor.authorYoonJeong Kim-
dc.contributor.authorH J Park-
dc.contributor.authorJong Suk Lee-
dc.contributor.authorSu Nam Gwak-
dc.contributor.authorWoo Hyuk Jung-
dc.contributor.authorSeung Goo Lee-
dc.contributor.authorDoo Il Kim-
dc.contributor.authorY C Lee-
dc.contributor.authorTae Kwang Oh-
dc.date.accessioned2017-04-19T09:12:03Z-
dc.date.available2017-04-19T09:12:03Z-
dc.date.issued2008-
dc.identifier.issn0021-9258-
dc.identifier.uri10.1074/jbc.M804092200ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8669-
dc.description.abstractTriphenylmethane dyes are aromatic xenobiotic compounds that are widely considered to be one of the main culprits of environmental pollution. Triphenylmethane reductase (TMR) from Citrobacter sp. strain KCTC 18061P was initially isolated and biochemically characterized as an enzyme that catalyzes the reduction of triphenylmethane dyes. Information from the primary amino acid sequence suggests that TMR is a dinucleotide-binding motif-containing enzyme; however, no other functional clues can be derived from sequence analysis. We present the crystal structure of TMR in complex with NADP+ at 2.0-A resolution. Despite limited sequence similarity, the enzyme shows remarkable structural similarity to short-chain dehydrogenase/reductase (SDR) family proteins. Functional assignments revealed that TMR has features of both classic and extended SDR family members and does not contain a conserved active site. Thus, it constitutes a novel class of SDR family proteins. On the basis of simulated molecular docking using the substrate malachite green and the TMR/NADP+ crystal structure, together with site-directed mutagenesis, we have elucidated a potential molecular mechanism for triphenylmethane dye reduction.-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.titleStructural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase-
dc.title.alternativeStructural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase-
dc.typeArticle-
dc.citation.titleJournal of Biological Chemistry-
dc.citation.number46-
dc.citation.endPage31990-
dc.citation.startPage31981-
dc.citation.volume283-
dc.contributor.affiliatedAuthorMyung Hee Kim-
dc.contributor.affiliatedAuthorYoonJeong Kim-
dc.contributor.affiliatedAuthorJong Suk Lee-
dc.contributor.affiliatedAuthorSu Nam Gwak-
dc.contributor.affiliatedAuthorWoo Hyuk Jung-
dc.contributor.affiliatedAuthorSeung Goo Lee-
dc.contributor.affiliatedAuthorDoo Il Kim-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.alternativeName김명희-
dc.contributor.alternativeName김윤정-
dc.contributor.alternativeName박효정-
dc.contributor.alternativeName이종석-
dc.contributor.alternativeName곽수남-
dc.contributor.alternativeName정우혁-
dc.contributor.alternativeName이승구-
dc.contributor.alternativeName김두일-
dc.contributor.alternativeName이영춘-
dc.contributor.alternativeName오태광-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, vol. 283, no. 46, pp. 31981-31990-
dc.identifier.doi10.1074/jbc.M804092200-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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