Ketopantoyl lactone reductase is a conjugated polyketone reductase

H Hata; S Shimizu; S Hattori; H Yamada

doi:10.1111/j.1574-6968.1989.tb03023.x

Ketopantoyl lactone reductase is a conjugated polyketone reductase

FEMS Microbiol Lett. 1989 Mar;49(1):87-90. doi: 10.1111/j.1574-6968.1989.tb03023.x.

Authors

H Hata¹, S Shimizu, S Hattori, H Yamada

Affiliation

¹ Department of Agricultural Chemistry, Kyoto University, Japan.

PMID: 2656398
DOI: 10.1111/j.1574-6968.1989.tb03023.x

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alcohol Oxidoreductases / classification*
Ketones / metabolism*
Mucor / enzymology
Oxidation-Reduction
Substrate Specificity

Substances

Ketones
Alcohol Oxidoreductases
2-oxopantoyl lactone reductase