| Literature DB >> 12596862 |
Michihiko Kataoka1, Atsushi Kotaka, Akiko Hasegawa, Masaru Wada, Ayumi Yoshizumi, Shigeru Nakamori, Sakayu Shimizu.
Abstract
Microorganisms were screened for ones that reduced 3,5,5-trimethyl-2-cyclohexene-1,4-dione (ketoisophorone; KIP), and several strains were found to produce (6R)-2,2,6-trimethylcyclohexane-1,4-dione (levodione). The enzyme catalyzing the reduction of the C=C bond of KIP to yield (6R)-levodione was isolated from Candida macedoniensis AKU4588. The results of primary structural analysis and its enzymatic properties suggested that the enzyme might be an Old Yellow Enzyme family protein.Entities:
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Year: 2002 PMID: 12596862 DOI: 10.1271/bbb.66.2651
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043