Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology.
|Abstract||Carbonyl groups are frequently found in endogenous or xenobiotic compounds. Reactive carbonyls, formed during lipid peroxidation or food processing, and xenobiotic quinones are able to covalently modify DNA or amino acids. They can also promote oxidative stress, the products of which are thought to be an important initiating factor in degenerative diseases or cancer. Carbonyl groups are reduced by an array of distinct NADPH-dependent enzymes, bel ... [truncated at 450 characters in length]|
|Subject||Alcohol Oxidoreductases Animals Humans Mammals NADH, NADPH Oxidoreductases Oxidative Stress Quinones Structure-Activity Relationship Xenobiotics metabolism physiology metabolism metabolism|
Structural basis for substrate specificity in human monomeric carbonyl reductases.
|Abstract||Carbonyl reduction constitutes a phase I reaction for many xenobiotics and is carried out in mammals mainly by members of two protein families, namely aldo-keto reductases and short-chain dehydrogenases/reductases. In addition to their capacity to reduce xenobiotics, several of the enzymes act on endogenous compounds such as steroids or eicosanoids. One of the major carbonyl reducing enzymes found in humans is carbonyl reductase 1 (CBR1) with a v ... [truncated at 450 characters in length]|
|Author||Pilka, Ewa S; Niesen, Frank H; Lee, Wen Hwa; et al|
|Subject||Alcohol Oxidoreductases Antineoplastic Agents Cloning, Molecular Crystallography, X-Ray Ethanolamines Humans Isoquinolines Kinetics Mutagenesis Mutagenesis, Site-Directed Structure-Activity Relationship Substrate Specificity Temperature Xenobiotics chemistry pharmacology methods chemistry chemistry chemistry|