title: Purification and characterization of N-ethylmaleimide reducing enzyme from Candida lipolytica.
abstract: N-Ethylmaleimide (NEM) reducing enzyme was purified to homogeneity from cell-free extracts of Candida lipolytica by chromatography techniques. The molecular weight of the native enzyme was estimated to be about 43,000 by gel filtration using Superose 12 and to be 47,000 by SDS-PAGE. This enzyme can use both NADPH and NADH as an electron donor, and catalyzes the reduction of the carbon-carbon double bond of five membered ring compounds which have two conjugated carbonyl groups on both sides of a double bond.
authors.affiliation: Department of Pharmaceutical Sciences, Tohoku University Hospital, Miyagi.
authors.forename: M
authors.initials: M
authors.lastname: Mizugaki
authors.forename: M
authors.initials: M
authors.lastname: Nakazawa
authors.forename: H
authors.initials: H
authors.lastname: Yamamoto
authors.forename: H
authors.initials: H
authors.lastname: Yamanaka
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002175:Candida / Q000201:enzymology*; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D005033:Ethylmaleimide / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008968:Molecular Conformation; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D010088:Oxidoreductases; C040723:alpha,beta-ketoalkene reductase; D005033:Ethylmaleimide