IPR015590
Aldehyde dehydrogenase domain
InterPro entry
Short name | Aldehyde_DH_dom |
Overlapping homologous superfamilies | |
domain relationships |
Description
Aldehyde dehydrogenases (
1.2.1.3 and
1.2.1.5) are enzymes that oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor. In mammals at least four different forms of the enzyme are known
[1]: 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. 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 entry.
Some of the proteins in this entry are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.
The allergens in this family include allergens with the following designations: Alt a 10 and Cla h 3.
References
1.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. Hempel J, Harper K, Lindahl R. Biochemistry 28, 1160-7, (1989). View articlePMID: 2713359
GO terms
Cross References
ENZYME
- 1.1.1.1
- 1.1.1.257
- 1.2.1.-
- 1.2.1.10
- 1.2.1.16
- 1.2.1.19
- 1.2.1.21
- 1.2.1.22
- 1.2.1.24
- 1.2.1.26
- 1.2.1.27
- 1.2.1.28
- 1.2.1.3
- 1.2.1.31
- 1.2.1.32
- 1.2.1.36
- 1.2.1.39
- 1.2.1.4
- 1.2.1.41
- 1.2.1.46
- 1.2.1.47
- 1.2.1.48
- 1.2.1.5
- 1.2.1.54
- 1.2.1.60
- 1.2.1.64
- 1.2.1.65
- 1.2.1.67
- 1.2.1.68
- 1.2.1.69
- 1.2.1.7
- 1.2.1.71
- 1.2.1.73
- 1.2.1.76
- 1.2.1.77
- 1.2.1.78
- 1.2.1.79
- 1.2.1.8
- 1.2.1.81
- 1.2.1.82
- 1.2.1.83
- 1.2.1.85
- 1.2.1.86
- 1.2.1.87
- 1.2.1.88
- 1.2.1.89
- 1.2.1.9
- 1.2.1.90
- 1.2.1.91
- 1.2.1.92
- 1.2.1.94
- 1.2.1.96
- 1.2.1.97
- 1.2.1.98
- 1.2.99.10
- 1.5.1.6
- 1.5.5.2
- 2.7.2.11
- 3.3.2.12
Genome Properties
- GenProp1529
- GenProp1678
- GenProp1425
- GenProp1402
- GenProp1715
- GenProp0457
- GenProp1267
- GenProp1551
- GenProp1226
- GenProp1589
- GenProp1321
- GenProp1502
- GenProp1276
- GenProp1390
- GenProp1437
- GenProp1434
- GenProp1401
- GenProp1370
- GenProp1762
- GenProp0715
- GenProp0717
- GenProp0292
- GenProp1497
- GenProp1677
- GenProp0294
- GenProp1620
- GenProp1297
- GenProp1487
- GenProp1379
Contributing Member Database Entry
- Pfam:PF00171
Representative structure
3vz3: Structural insights into substrate and cofactor selection by sp2771