title: Autocatalytic modification of human carbonyl reductase by 2-oxocarboxylic acids.
abstract: Carbonyl reductase occurs in multiple molecular forms. Sequence analysis has yielded a carboxyethyllysine residue in one of the enzyme forms, suggesting that pyruvate has been incorporated in a posttranslational enzymatic reaction [Krook, M., Ghosh, D., Strömberg R., Carlquist, M. and Jörnvall, H. (1993) Proc. Natl. Acad. Sci. USA 90, 502-506]. Using highly purified carbonyl reductase from human brain we show that pyruvate and other 2-oxocarboxylic acids are bound to the enzyme in an autocatalytic reaction. The resulting enzyme forms were indistinguishable from the native enzyme forms by electrophoresis and isoelectric focusing.
authors.affiliation: Chemisches Zentrallabor der Universitätskliniken, Inselspital, Bern, Switzerland.
authors.forename: B
authors.initials: B
authors.lastname: Wermuth
authors.forename: K M
authors.initials: KM
authors.lastname: Bohren
authors.forename: E
authors.initials: E
authors.lastname: Ernst
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D001921:Brain / Q000201:enzymology; D002264:Carboxylic Acids / Q000737:chemistry*; D002384:Catalysis; D006801:Humans; D007651:Keto Acids / Q000737:chemistry; D011773:Pyruvates / Q000737:chemistry; D019289:Pyruvic Acid
chemical_list: D002264:Carboxylic Acids; D007651:Keto Acids; D011773:Pyruvates; D019289:Pyruvic Acid; D000429:Alcohol Oxidoreductases