Structural basis for substrate specificity in human monomeric carbonyl reductases.

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 en...

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Bibliografische gegevens
Hoofdauteurs:	Pilka, E, Niesen, F, Lee, W, El-Hawari, Y, Dunford, J, Kochan, G, Wsol, V, Martin, H, Maser, E, Oppermann, U
Formaat:	Journal article
Taal:	English
Gepubliceerd in:	2009
Onderwerpen:	methods chemistry Isoquinolines Humans Crystallography, X-Ray Cloning, Molecular Xenobiotics Substrate Specificity Kinetics Mutagenesis, Site-Directed Structure-Activity Relationship Alcohol Oxidoreductases Mutagenesis Ethanolamines pharmacology Temperature Antineoplastic Agents

Structural basis for substrate specificity in human monomeric carbonyl reductases. door Pilka, E, Niesen, F, Lee, W, El-Hawari, Y, Dunford, J, Kochan, G, Wsol, V, Martin, H, Maser, E, Oppermann, U

Gepubliceerd in 2009

Journal article

Structural basis for substrate specificity in human monomeric carbonyl reductases.

Structural basis for substrate specificity in human monomeric carbonyl reductases. door Pilka, E, Niesen, F, Lee, W, El-Hawari, Y, Dunford, J, Kochan, G, Wsol, V, Martin, H, Maser, E, Oppermann, U

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