Ketopantoyl lactone reductase is a conjugated polyketone reductase.
Ketopantoyl lactone reductase (EC 1.1.1.168) of Saccharomyces cerevisiae was found to catalyze the reduction of a variety of natural and unnatural conjugated polyketone compounds and quinones, such as isatin, ninhydrin, camphorquinone and beta-naphthoquinone in the presence of NADPH. 5-Bromoisatin is the best substrate for the enzyme (Km = 3.1 mM; Vmax = 650 mumol/min/mg). The enzyme is inhibited by quercetin, and several polyketones. These results suggest that ketopantoyl lactone reductase is a carbonyl reductase which specifically catalyzes the reduction of conjugated polyketones.
Hata
H
H
Department of Agricultural Chemistry, Kyoto University, Japan.
Shimizu
S
S
Hattori
S
S
Yamada
H
H
D000429:Alcohol Oxidoreductases / Q000145:classification*; D007659:Ketones / Q000378:metabolism*; D009089:Mucor / Q000201:enzymology; D010084:Oxidation-Reduction; D013379:Substrate Specificity
D007659:Ketones; D000429:Alcohol Oxidoreductases; C021935:2-oxopantoyl lactone reductase