Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.
|Abstract||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 othe ... [truncated at 450 characters in length]|
|Author||El-Hawari, Yasser; Favia, Angelo D; Pilka, Ewa S; et al|
|Subject||Alcohol Oxidoreductases Amino Acid Sequence Base Sequence Binding Sites Biocatalysis DNA Primers DNA, Complementary Humans Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Sequence Homology, Amino Acid Substrate Specificity chemistry genetics isolation and purification metabolism|
Development of homogeneous luminescence assays for histone demethylase catalysis and binding.
|Abstract||Covalent modifications to histones play important roles in chromatin dynamics and the regulation of gene expression. The JumonjiC (JmjC)-containing histone demethylases (HDMs) catalyze the demethylation of methylated lysine residues on histone tails. Here we report the development of homogeneous luminescence-based assay methods for measuring the catalytic activity and the binding affinities of peptides to HDMs. The assays use amplified luminescen ... [truncated at 450 characters in length]|
|Author||Kawamura, Akane; Tumber, Anthony; Rose, Nathan R; et al|
|Subject||Biocatalysis Enzyme Inhibitors Humans Jumonji Domain-Containing Histone Demethylases Luminescent Measurements Peptides Protein Binding Protein Isoforms Protein Structure, Tertiary chemistry pharmacology metabolism methods chemistry metabolism|