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  • Title: A novel NADPH-dependent carbonyl reductase of Candida macedoniensis: purification and characterization.
    Author: Kataoka M, Doi Y, Sim TS, Shimizu S, Yamada H.
    Journal: Arch Biochem Biophys; 1992 May 01; 294(2):469-74. PubMed ID: 1567202.
    Abstract:
    A novel NADPH-dependent carbonyl reductase was purified to homogeneity from the soluble fraction of a cell extract of Candida macedoniensis AKU 4588. The enzyme catalyzes not only the reduction of quinones, but also the reduction of aromatic aldehydes, conjugated polyketones, 2'-ketopantothenate esters, and 4-chloro-3-oxobutanoate esters. The enzyme shows absolute specificity for NADPH as a coenzyme and also shows quite high affinity toward NADPH (Km less than 5 microM). The apparent Km values for menadione and p-toluquinone are 167 and 180 microM, respectively. The enzyme is not a flavoprotein and is a monomer protein with a relative molecular mass of 45,000. Dicoumarol, quercetin, and some sulfhydryl reagents inhibit the enzyme activity.
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