Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0014-5793(99)00520-7
DC FieldValue
dc.titleCharacterization of a novel cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida ML2
dc.contributor.authorFong, K.P.Y.
dc.contributor.authorTan, H.-M.
dc.date.accessioned2012-03-28T05:50:37Z
dc.date.available2012-03-28T05:50:37Z
dc.date.issued1999
dc.identifier.citationFong, K.P.Y., Tan, H.-M. (1999). Characterization of a novel cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida ML2. FEBS Letters 451 (1) : 5-9. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(99)00520-7
dc.identifier.issn00145793
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/31313
dc.description.abstractA second and novel cis-benzene dihydrodiol dehydrogenase which is able to dehydrogenate a range of cis-dihydrodiols and other vicinal alcohols has been purified from Pseudomonas putida ML2. The enzyme is a tetramer of a polypeptide of 39 kDa in molecular mass and has a pH optimum of 9.0. Despite having a primary structure that has significant similarity to glycerol dehydrogenases, the k(cat)/K(m) value of the enzyme for cis-benzene dihydrodiol is 4300-fold higher compared to glycerol. The apparent K(m) values of the enzyme for cis-benzene dihydrodiol and glycerol are 0.01 mM and 46 mM, respectively, and 0.22 mM for NAD+. Copyright (C) 1999 Federation of European Biochemical Societies.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0014-5793(99)00520-7
dc.sourceScopus
dc.subjectBenzene catabolism
dc.subjectcis-Benzene dihydrodiol dehydrogenase
dc.subjectPseudomonas putida ML2
dc.subjectType III alcohol dehydrogenase
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1016/S0014-5793(99)00520-7
dc.description.sourcetitleFEBS Letters
dc.description.volume451
dc.description.issue1
dc.description.page5-9
dc.description.codenFEBLA
dc.identifier.isiut000080472900002
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