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InterPro: IPR012394 Aldehyde dehydrogenase NAD(P)-dependent
Protein matches
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UniProtKB Matches: 1093 proteins |
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Accession
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IPR012394 Aldehyde_DH_NAD(P) |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR015590 Aldehyde dehydrogenase
IPR016160 Aldehyde dehydrogenase, conserved site
IPR016162 Aldehyde dehydrogenase, N-terminal
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GO Term annotation
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Process
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GO:0006081 cellular aldehyde metabolic process
GO:0055114 oxidation reduction
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Function
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GO:0004030 aldehyde dehydrogenase [NAD(P)+] activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Aldehydes are produced as intermediates during the metabolism of many different compounds including amino acids, carbohydrates, lipids vitamins and steroids [1]. They are highly reactive compounds whose buildup to excess levels can cause cytotoxic, genotoxic and carcinogenic effects. Aldehyde dehydrogenases oxidise these compounds to their respective carboxylic acids. This is necessary both for the operation of these metabolic pathways, and to prevent the concentration of aldehydes within the cell from reaching toxic levels.
Proteins in this entry are NAD(P)-dependent aldehyde dehydrogenases, found in a variety of organisms, including general aldehyde dehydrogensases (EC:1.2.1.5), fatty aldehyde dehydrogenases (EC:1.2.1.3), and coniferyl aldehyde dehydrogenase (EC:1.2.1.68). Structural studies of the Rattus norvegicus protein (P11883) show that this enzyme is a homodimer where each subunit consists of two alpha-beta-alpha domains [2]. The mode of NAD binding differs substantially from that commonly associated with the Rossman fold.
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Structural links
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Database links
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Publications
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1.
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Vasiliou V, Pappa A, Petersen DR.
Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism.
Chem. Biol. Interact. 129 1-19 2000
[PubMed: 11154732]
http://dx.doi.org/10.1016/S0009-2797(00)00211-8
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2.
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Liu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC.
The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.
Nat. Struct. Biol. 4 317-26 1997
[PubMed: 9095201]
http://dx.doi.org/10.1038/nsb0497-317
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InterPro 23.1
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