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Autocatalytic modification of human carbonyl reductase by 2‐oxocarboxylic acids
Author(s) -
Wermuth Bendicht,
Bohren Kurt M.,
Ernst Elsbeth
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80719-b
Subject(s) - autocatalysis , chemistry , enzyme , biochemistry , isoelectric point , reductase , stereochemistry , isoelectric focusing , catalysis
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.