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Aldehyde dehydrogenase (NAD+)

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aldehyde dehydrogenase (NAD)
Aldehyde dehydrogenase tetramer, Human
Identifiers
EC no.1.2.1.3
CAS no.9028-86-8
Databases
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BRENDABRENDA entry
ExPASyNiceZyme view
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MetaCycmetabolic pathway
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In enzymology, an aldehyde dehydrogenase (NAD+) (EC 1.2.1.3) is an enzyme that catalyzes the chemical reaction

an aldehyde + NAD + H2O {\displaystyle \rightleftharpoons } an acid + NADH + H

The 3 substrates of this enzyme are aldehyde, NAD, and H2O, whereas its 3 products are acid, NADH, and H.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aldehyde:NAD+ oxidoreductase. Other names in common use include CoA-independent aldehyde dehydrogenase, m-methylbenzaldehyde dehydrogenase, NAD-aldehyde dehydrogenase, NAD-dependent 4-hydroxynonenal dehydrogenase, NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, propionaldehyde dehydrogenase, and aldehyde dehydrogenase (NAD). This enzyme participates in 17 metabolic pathways: glycolysis / gluconeogenesis, ascorbate and aldarate metabolism, fatty acid metabolism, bile acid biosynthesis, urea cycle and metabolism of amino groups, valine, leucine and isoleucine degradation, lysine degradation, histidine metabolism, tryptophan metabolism, beta-alanine metabolism, glycerolipid metabolism, pyruvate metabolism, 1,2-dichloroethane degradation, propanoate metabolism, 3-chloroacrylic acid degradation, butanoate metabolism, and limonene and pinene degradation.

References

External links

Aldehyde/oxo oxidoreductases (EC 1.2)
1.2.1: NAD or NADP
1.2.2: cytochrome
1.2.3: oxygen
1.2.4: disulfide
1.2.7: iron–sulfur protein
Enzymes
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Regulation
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Kinetics
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