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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
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