Enzyme reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1989-08

AUTHORS

W. Dangel, A. Tschech, G. Fuchs

ABSTRACT

The enzymes involved in the anaerobic degradation of cyclohexanol were searched for in a denitrifying Pseudomonas species which metabolizes this alicyclic compound to CO2 anaerobically. All postulated enzyme activities were demonstrated in vitro with sufficient specific activities. Cyclohexanol dehydrogenase catalyzes the oxidation of the substrate to cyclohexanone. Cyclohexanone dehydrogenase oxidizes cyclohexanone to 2-cyclohexenone. 2-Cyclohexenone hydratase and 3-hydroxycyclohexanone dehydrogenase convert 2-cyclohexenone via 3-hydroxycyclohexanone into 1,3-cyclohexanedione. Finally, the dione is cleaved by 1,3-cyclohexanedione hydrolase into 5-oxocaproic acid. Some kinetic and regulatory properties of these enzymes were studied. More... »

PAGES

273-279

Journal

TITLE

Archives of Microbiology

ISSUE

3

VOLUME

152

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00409663

    DOI

    http://dx.doi.org/10.1007/bf00409663

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1037468748

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/2505723


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