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

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 CB...

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Bibliographic Details
Main Authors:	El-Hawari, Y, Favia, A, Pilka, E, Kisiela, M, Oppermann, U, Martin, H, Maser, E
Format:	Journal article
Language:	English
Published:	2009
Subjects:	DNA Primers Base Sequence chemistry Models, Molecular Kinetics Substrate Specificity genetics Humans Sequence Homology, Amino Acid Binding Sites DNA, Complementary Alcohol Oxidoreductases Amino Acid Sequence metabolism Mutagenesis, Site-Directed isolation and purification Biocatalysis Molecular Sequence Data

Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis. by El-Hawari, Y, Favia, A, Pilka, E, Kisiela, M, Oppermann, U, Martin, H, Maser, E

Published 2009

Journal article

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

Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis. by El-Hawari, Y, Favia, A, Pilka, E, Kisiela, M, Oppermann, U, Martin, H, Maser, E

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