Literature DB >> 8253186

Autocatalytic modification of human carbonyl reductase by 2-oxocarboxylic acids.

B Wermuth1, K M Bohren, E Ernst.   

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.

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Year:  1993        PMID: 8253186     DOI: 10.1016/0014-5793(93)80719-b

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Mutation of threonine-241 to proline eliminates autocatalytic modification of human carbonyl reductase.

Authors:  M A Sciotti; S Nakajin; B Wermuth; M E Baker
Journal:  Biochem J       Date:  2000-08-15       Impact factor: 3.857

2.  Pharmacogenetics of human carbonyl reductase 1 (CBR1) in livers from black and white donors.

Authors:  Vanessa Gonzalez-Covarrubias; Jianping Zhang; James L Kalabus; Mary V Relling; Javier G Blanco
Journal:  Drug Metab Dispos       Date:  2008-11-20       Impact factor: 3.922

  2 in total

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