Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.

Journal article

Human carbonyl reductase is a member of the short-chain dehydrogenase/reductase (SDR) protein superfamily and is known to play an important role in the detoxification of xenobiotics bearing a carbonyl group. The two monomeric NADPH-dependent human isoforms of cytosolic carbonyl reductase CBR1 and CBR3 show a sequence similarity of 85% on the amino acid level, which is definitely high if compared to the low similarities usually observed among other members of the SDR superfamily (15-30%). Desp...

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Authors: El-Hawari, Y; Favia, A; Pilka, E; Kisiela, M; Oppermann, U

• Publication status: Published
• Journal: Chemico-biological interactions
• Volume: 178
• Issue: 1-3
• Pages: 234-241
• Publication date: 2009-03-01
• DOI: 10.1016/j.cbi.2008.11.004
• EISSN: 1872-7786
• ISSN: 0009-2797
• Language: English
• Keywords: Kinetics; Molecular Sequence Data; Sequence Homology, Amino Acid; DNA, Complementary; Binding Sites; Substrate Specificity; Mutagenesis, Site-Directed; Base Sequence; Biocatalysis; DNA Primers; Amino Acid Sequence; Alcohol Oxidoreductases; Models, Molecular; Humans