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|Title:||Characterization of a novel cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida ML2||Authors:||Fong, K.P.Y.
cis-Benzene dihydrodiol dehydrogenase
Pseudomonas putida ML2
Type III alcohol dehydrogenase
|Issue Date:||1999||Citation:||Fong, 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||Abstract:||A 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.||Source Title:||FEBS Letters||URI:||http://scholarbank.nus.edu.sg/handle/10635/31313||ISSN:||00145793||DOI:||10.1016/S0014-5793(99)00520-7|
|Appears in Collections:||Staff Publications|
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