Cytoplasmic Aldo-Keto Reductases: A Class of Drug Metabolizing Enzymes
- 13 August 1976
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 193 (4253), 595-597
- https://doi.org/10.1126/science.959821
Abstract
Aldehyde and ketone xenobiotic substances are preferentially reduced to alcohols by cytoplasmic enzymes in mammals. These enzymes are widely distributed in the tissues, have broad substrate specificities, have similar physical-chemical characteristics, and require reduced nicotinamide adenine dinucleotide as cofactor for the reductions. These reductases define a system of detoxification for aldehyde and ketone groups.This publication has 12 references indexed in Scilit:
- Studies on a ketone reductase in human and rat liver and kidney soluble fraction using warfarin as a substrateBiochemical Pharmacology, 1975
- Dihydromorphinone ketone reductasesLife Sciences, 1975
- The Partial Purification and Properties of a Human Erythrocyte 4-Nitroacetophenone ReductaseXenobiotica, 1975
- Rat Liver Daunorubicin ReductasePublished by Elsevier ,1974
- Bunolol Metabolism by Cell-Free Preparations of Human Liver: Biosynthesis of DihydrobunololXenobiotica, 1972
- Reduction of Ketones in Liver CytosolXenobiotica, 1971
- Reductase for Aromatic Aldehydes and KetonesPublished by Elsevier ,1968
- Enzymic Studies on TPN L-Hexonate Dehydrogenase from Rat LiverThe Journal of Biochemistry, 1961
- Studies in detoxication. 69. The metabolism of alkylbenzenes: n-propylbenzene and n-butylbenzene with further observations on ethylbenzeneBiochemical Journal, 1956
- Studies in detoxication. 56. The metabolism of alkylbenzenes. Stereochemical aspects of the biological hydroxylation of ethylbenzene to methylphenylcarbinolBiochemical Journal, 1954