Characterization of a novel cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida ML2.
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 kcat/Km value of the enzyme for cis-benzene dihydrodiol is 4300-fold higher compared to glycerol. The apparent Km values of the enzyme for cis-benzene dihydrodiol and glycerol are 0.01 mM and 46 mM, respectively, and 0.22 mM for NAD+.
Fong
K P
KP
Department of Microbiology, National University of Singapore, Singapore.
Tan
H M
HM
D000595:Amino Acid Sequence; D004795:Enzyme Stability; D007700:Kinetics; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D016958:Pseudomonas putida / Q000201:enzymology*; D013379:Substrate Specificity
D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C020054:cis-1,2-dihydrobenzene-1,2-diol dehydrogenase