A group of NAD(P)+-dependent enzymes that catalyze the oxidation of aldehydes to their corresponding acids. Nineteen forms exist in humans and they are present in all tissues. Aldehydes are abundant in nature and can be generated during normal metabolism or from metabolism of exogenous drugs and environmental substrates. Several of these enzymes are important in detoxification of anticancer drugs.
Aldehyde dehydrogenase (ALDH) isoenzymes are found in all cell types and play an essential role in the removal of toxic aldehydes as well as the production of active molecules. Aldehydes are abundant in nature and come from normal endogenous metabolism or from ingested materials or environmental sources. Examples include the removal of aldehydes produced from alcohol ingestion and toxic aldehdyes from smoke. Some ALDH isoenzymes are involved in the synthesis of retinoic acid (from Vitamin A) and purines as well as the metabolism of corticosteroids and...
KeywordsRetinoic Acid Acute Promyelocytic Leukemia ALDH Activity Succinic Semialdehyde ALDH Gene
- (2012) Immunodeficient NUDE MICE. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1816. doi: 10.1007/978-3-642-16483-5_2986Google Scholar
- (2012) Neurotransmitters. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 2505. doi: 10.1007/978-3-642-16483-5_4049Google Scholar
- Johnson BA (2015) Disulfiram. In: Stolerman IP, Price LH (ed) Encyclopedia of psychopharmacology. Springer, Berlin/Heidelberg, pp 531–534. doi: 10.1007/978-3-642-36172-2_172Google Scholar
- http://ghr.nlm.nih.gov/condition/hyperprolinemiaGoogle Scholar
- http://ghr.nlm.nih.gov/condition/pyridoxine-dependent-epilepsyGoogle Scholar
- http://ghr.nlm.nih.gov/condition/sjogren-larsson-syndromeGoogle Scholar
- http://ghr.nlm.nih.gov/condition/succinic-semialdehyde-dehydrogenase-deficiencyGoogle Scholar