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Alpha-santonin 1,2-reductase and its role in the formation of dihydrosantonin and lumisantonin by Pseudomonas cichorii S

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dc.contributor.author Naik, U.P.
dc.contributor.author Mavinkurve, S.
dc.date.accessioned 2015-06-02T09:58:06Z
dc.date.available 2015-06-02T09:58:06Z
dc.date.issued 1987
dc.identifier.citation Canadian Journal of Microbiology. 33(8); 1987; 658-662. en_US
dc.identifier.uri http://dx.doi.org/10.1139/m87-115
dc.identifier.uri http://irgu.unigoa.ac.in/drs/handle/unigoa/94
dc.description.abstract 1,2-Dihydrosantonin is the first stable product in the degradative pathway of alpha-santonin byPseudomonas cichorii S. Its formation is catalyzed by an oxidoreductase, which is NADH or NADPH dependent and has an apparent Km value of 66.66 mu M for santonin and 44.33 mu M for NADH. The enzyme activity is stable at pH 6.0, 7.0, and 8.0, and is not affected by EDTA and divalent metal ions. It is postulated that the enzymic reduction of santonin occurs via formation of a transient zwitterionic intermediate, which undergoes nonenzymatic 1,4-sigmatropic rearrangement to yield lumisantonin during the solvent extraction process. Lumisantonin is, thus, not a true metabolic intermediate but an artifact. en_US
dc.publisher NRC Research Press (Canadian Science Publishing) en_US
dc.subject Microbiology en_US
dc.title Alpha-santonin 1,2-reductase and its role in the formation of dihydrosantonin and lumisantonin by Pseudomonas cichorii S en_US
dc.type Journal article en_US
dc.identifier.impf y


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