Aldehyde dehydrogenases (EC 18.104.22.168 and EC 22.214.171.124) are enzymes which oxidize
a wide variety of aliphatic and aromatic aldehydes. In mammals at least four
different forms of the enzyme are known : class-1 (or Ald C) a tetrameric
cytosolic enzyme, class-2 (or Ald M) a tetrameric mitochondrial enzyme, class-3 (or Ald D) a dimeric cytosolic enzyme, and class IV a microsomal enzyme.
Aldehyde dehydrogenases have also been sequenced from fungal and bacterial
species. A number of enzymes are known to be evolutionary related to aldehyde
dehydrogenases; these enzymes are listed below.
Plants and bacterial βine-aldehyde dehydrogenase (EC 126.96.36.199) , an
enzyme that catalyzes the last step in the biosynthesis of βine.
Plants and bacterial NADP-dependent glyceraldehyde-3-phosphate
dehydrogenase (EC 188.8.131.52).
Escherichia coli succinate-semialdehyde dehydrogenase (NADP+) (EC 184.108.40.206)
(gene gabD) , which reduces succinate semialdehyde into succinate.
Pseudomonas putida 2-hydroxymuconic semialdehyde dehydrogenase  (genes
dmpC and xylG), an enzyme in the meta-cleavage pathway for the degradation
of phenols, cresols and catechol.
Bacterial and mammalian methylmalonate-semialdehyde dehydrogenase (MMSDH)
(EC 220.127.116.11) , an enzyme involved in the distal pathway of valine
Yeast delta-1-pyrroline-5-carboxylate dehydrogenase (EC 18.104.22.168)  (gene
PUT2), which converts proline to glutamate.
Bacterial multifunctional putA protein, which contains a delta-1-pyrroline-
5-carboxylate dehydrogenase domain.
26G, a garden pea protein of unknown function which is induced by
dehydration of shoots .
Mammalian formyltetrahydrofolate dehydrogenase (EC 22.214.171.124) . This is a
cytosolic enzyme responsible for the NADP-dependent decarboxylative
reduction of 10-formyltetrahydrofolate into tetrahydrofolate. It is an
protein of about 900 amino acids which consist of three domains; the C-
terminal domain (480 residues) is structurally and functionally related to
Yeast hypothetical protein YBR006w.
Yeast hypothetical protein YER073w.
Yeast hypothetical protein YHR039c.
Caenorhabditis elegans hypothetical protein F01F1.6.
A glutamic acid and a cysteine residue have been implicated in the catalytic
activity of mammalian aldehyde dehydrogenase. These residues are conserved in
all the enzymes of this family. We have derived two patterns for this family,
one for each of the active site residues.
Omega-crystallins are minor structural components of squids and octopi
eye lens. They are evolutionary related to aldehyde dehydrogenases but have
lost their catalytic activity. These patterns will not detect them.
PROSITE methods (with tools and information) covered by this documentation:
Hempel J. Harper K. Lindahl R.
Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria.
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.