Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily.
BACKGROUND
Aldehydes are highly reactive molecules. While several non-P450 enzyme systems participate in their metabolism, one of the most important is the aldehyde dehydrogenase (ALDH) superfamily, composed of NAD(P)+-dependent enzymes that catalyze aldehyde oxidation.


OBJECTIVE
This article presents a review of what is currently known about each member of the human ALDH superfamily including the pathophysiological significance of these enzymes.


METHODS
Relevant literature involving all members of the human ALDH family was extensively reviewed, with the primary focus on recent and novel findings.


CONCLUSIONS
To date, 19 ALDH genes have been identified in the human genome and mutations in these genes and subsequent inborn errors in aldehyde metabolism are the molecular basis of several diseases, including Sjögren-Larsson syndrome, type II hyperprolinemia, gamma-hydroxybutyric aciduria and pyridoxine-dependent seizures. ALDH enzymes also play important roles in embryogenesis and development, neurotransmission, oxidative stress and cancer. Finally, ALDH enzymes display multiple catalytic and non-catalytic functions including ester hydrolysis, antioxidant properties, xenobiotic bioactivation and UV light absorption.
Marchitti
Satori A
SA
University of Colorado Health Sciences Center, Molecular Toxicology & Environmental Health Sciences Program, Department of Pharmaceutical Sciences, 4200 East Ninth Avenue, C238, Denver, Colorado 80262, USA.
Brocker
Chad
C
Stagos
Dimitrios
D
Vasiliou
Vasilis
V
D000444:Aldehyde Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism*; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D007527:Isoenzymes; D008661:Metabolism, Inborn Errors / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D010084:Oxidation-Reduction; D013379:Substrate Specificity
D000447:Aldehydes; D007527:Isoenzymes; D000444:Aldehyde Dehydrogenase