In:
Applied and Environmental Microbiology, American Society for Microbiology, Vol. 65, No. 12 ( 1999-12), p. 5242-5246
Abstract:
cis -Chlorobenzene dihydrodiol dehydrogenase (CDD) from Pseudomonas sp. strain P51, cloned into Escherichia coli DH5α(pTCB149) was able to oxidize cis -dihydrodihydroxy derivatives ( cis -dihydrodiols) of dihydronaphthalene, indene, and four para -substituted toluenes to the corresponding catechols. During the incubation of a nonracemic mixture of cis -1,2-indandiol, only the (+)- cis -(1 R ,2 S ) enantiomer was oxidized; the (−)- cis -( S ,2 R ) enantiomer remained unchanged. CDD oxidized both enantiomers of cis -1,2-dihydroxy-1,2,3,4-tetrahydronaphthalene, but oxidation of the (+)- cis -(1 S ,2 R ) enantiomer was delayed until the (−)- cis -(1 R ,2 S ) enantiomer was completely depleted. When incubated with nonracemic mixtures of para -substituted cis -toluene dihydrodiols, CDD always oxidized the major enantiomer at a higher rate than the minor enantiomer. When incubated with racemic 1-indanol, CDD enantioselectively transformed the (+)-(1 S ) enantiomer to 1-indanone. This stereoselective transformation shows that CDD also acted as an alcohol dehydrogenase. Additionally, CDD was able to oxidize (+)- cis -(1 R ,2 S )-dihydroxy-1,2-dihydronaphthalene, (+)- cis -monochlorobiphenyl dihydrodiols, and (+)- cis -toluene dihydrodiol to the corresponding catechols.
Type of Medium:
Online Resource
ISSN:
0099-2240
,
1098-5336
DOI:
10.1128/AEM.65.12.5242-5246.1999
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
1999
detail.hit.zdb_id:
223011-2
detail.hit.zdb_id:
1478346-0
SSG:
12
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