Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone.
Michihiko Kataoka, Atsushi Kotaka, Akiko Hasegawa, Masaru Wada, Ayumi Yoshizumi, Shigeru Nakamori, Sakayu Shimizu
Index: Biosci. Biotechnol. Biochem. 66(12) , 2651-7, (2002)
Full Text: HTML
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.
Related Compounds
Related Articles:
2015-06-16
[Anal. Chem. 87 , 6335-41, (2015)]
2005-10-01
[Food Addit. Contam. 22(10) , 1012-22, (2005)]
The synthesis and spectral properties of a stimuli-responsive D-π-A charge transfer dye.
2011-01-01
[Spectrochim. Acta. A. Mol. Biomol. Spectrosc. 78(1) , 234-7, (2011)]
2007-06-29
[J. Chromatogr. A. 1155(1) , 100-4, (2007)]
Toxicology and carcinogenesis studies of isophorone in F344 rats and B6C3F1 mice.
1986-05-01
[Toxicology 39(2) , 207-19, (1986)]