Characterization of a Novel Cis-Benzene Dihydrodiol Dehydrogenase From Pseudomonas Putida ML2

FEBS Lett. 1999 May 14;451(1):5-9. doi: 10.1016/s0014-5793(99)00520-7.


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+.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Enzyme Stability
  • Kinetics
  • Molecular Sequence Data
  • Oxidoreductases / chemistry
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Oxidoreductases Acting on CH-CH Group Donors*
  • Pseudomonas putida / enzymology*
  • Substrate Specificity


  • Oxidoreductases
  • Oxidoreductases Acting on CH-CH Group Donors
  • cis-1,2-dihydrobenzene-1,2-diol dehydrogenase