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. 2005 Jun;2(2):138-43.
doi: 10.1186/1479-7364-2-2-138.

Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family

Vasilis Vasiliou  1 , Daniel W Nebert
Affiliations

Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family

Vasilis Vasiliou et al. Hum Genomics. 2005 Jun.

Abstract

The aldehyde dehydrogenase (ALDH) gene superfamily encodes enzymes that are critical for certain life processes and detoxification via the NAD(P)(+)-dependent oxidation of numerous endogenous and exogenous aldehyde substrates, including pharmaceuticals and environmental pollutants. Analysis of the ALDH gene superfamily in the latest databases showed that the human genome contains 19 putatively functional genes and three pseudogenes. A number of ALDH genes are upregulated as a part of the oxidative stress response and inexplicably overexpressed in various tumours, leading to problems during cancer chemotherapy. Mutations in ALDH genes cause inborn errors of metabolism--such as the Sjögren-Larsson syndrome, type II hyperprolinaemia and gamma-hydroxybutyric aciduria--and are likely to contribute to several complex diseases, including cancer and Alzheimer's disease. The ALDH gene products appear to be multifunctional proteins, possessing both catalytic and non-catalytic properties.

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Figures

Figure 1
Figure 1
Multiple functions of aldehyde dehydrogenase (ALDH) enzymes. Endobiotics, endogenous compounds. Xenobiotics, foreign chemicals.
Figure 2
Figure 2
Dendrogram of the 19 human aldehyde dehydrogenase (ALDH) genes that are bona fide members of the ALDH superfamily. To avoid additional clutter, alternative splice variants of ALDH genes have not been included in the construction of this tree or the three pseudogenes listed in Table 1. This neighbour-joining method gives various branches of different lengths, reflecting that evolutionary divergence is not the same between different branches of the gene tree.
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