Selectivity Studies of the Benzene cis -Dihydrodiol Dehydrogenase Enzyme from Pseudomonas putida ML2 with Vicinal Diol Substrates |
| |
| Authors: | Christopher C.R. Allen Claire E. Walker Narain D. Sharma Nuala A. Kerley Derek R. Boyd Howard Dalton |
| |
| Affiliation: | 1. Department of Biological Sciences, The University of Warwick, Coventry, CV4 7AL, UK;2. The QUESTOR Centre, Queens University of Belfast, Belfast, BT9 5AG, UK;3. School of Chemistry, The Queen's University of Belfast, Belfast, BT9 5AG, UK |
| |
| Abstract: | The enantiopure (1 S, 2 S )- cis -dihydrodiol metabolites 2B - 5B have been obtained in low yield from the corresponding monosubstituted halobenzene substrates 2A - 5A, using a wild-type strain of Pseudomonas putida (ML2) containing benzene dioxygenase (BDO). Benzene cis -dihydrodiol dehydrogenase (BCD) from P. putida ML2 and naphthalene cis -dihydrodiol dehydrogenase (NCD) from P. putida 8859 were purified and used in a comparative study of the stereoselective biotransformation of cis -dihydrodiol enantiomers 2B - 5B. The BCD and NCD enzymes were found to accept cis -dihydrodiol enantiomers of monosubstituted benzene cis -dihydrodiol substrates 2B - 5B of opposite absolute configuration. The acyclic alkene 1,2-diols 10 - 17 were also found to be acceptable substrates for BCD. |
| |
| Keywords: | Pseudomonas Putida Ml2 Biotransformations Biocatalysis Benzene cis -dihydrodiol Dehydrogenase |
|
|
