| Literature DB >> 10356973 |
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 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+.Entities:
Mesh：
Substances：
Year: 1999 PMID： 10356973 DOI： 10.1016/s0014-5793(99)00520-7
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124