cis-Chlorobenzene dihydrodiol dehydrogenase (TcbB) from Pseudomonas sp. strain P51, expressed in Escherichia coli DH5alpha (pTCB149), catalyzes enantioselective dehydrogenase reactions

Authors :: Raschke, Henning
Fleishmann, Thomas
Meer, Jan Roelof van der
Kohler, Hans-Peter E.
Source :: Applied and Environmental Microbiology. Dec, 1999, Vol. 65 Issue 12, p5242, 5 p.
Publication Year :: 1999
Abstract: Pseudomonas sp. strain P51 cis-chlorobenzene dihydrodiol dehydrogenase (CDD)(TcbB) expressed in Escherichia coli DH5alpha (pTCB149) has been found to catalyze enantioselective dehydrogenase reactions. The study was carried out with the object of investigating the potential of CDD for enantiomeric resolution of chiral dihydrodiols. CDD preferentially oxidized the para-halogenated cis-toluene dihydrodiol enantiomers preferentially formed by chlorobenzene dioxygenase (CDO).

Subjects :: Enantiomers -- Research
Dehydrogenases -- Research
Pseudomonas -- Physiological aspects
Escherichia coli -- Physiological aspects
Enzymes -- Physiological aspects
Cytochemistry -- Research
Biological sciences

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