Old Yellow Enzyme fromCandida macedoniensisCatalyzes the Stereospecific Reduction of the C=C Bond of Ketoisophorone | Zendy

Michihiko Kataoka | Zendy; Atsushi Kotaka | Zendy; Akiko Hasegawa | Zendy; Masaru Wada | Zendy; Ayumi Yoshizumi | Zendy; Shigeru Nakamori | Zendy; Sakayu Shimizu | Zendy

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Old Yellow Enzyme fromCandida macedoniensisCatalyzes the Stereospecific Reduction of the C=C Bond of Ketoisophorone

Author(s) -

Michihiko Kataoka,

Atsushi Kotaka,

Akiko Hasegawa,

Masaru Wada,

Ayumi Yoshizumi,

Shigeru Nakamori,

Sakayu Shimizu

Publication year - 2002

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.66.2651

Subject(s) - enzyme , stereospecificity , cyclohexene , chemistry , yield (engineering) , stereochemistry , biochemistry , catalysis , materials science , metallurgy

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.

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