Aldehyde dehydrogenase (NAD+)

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⁺

aldehyde dehydrogenase (NAD)
Aldehyde dehydrogenase tetramer, Human
Identifiers
EC no.	1.2.1.3
CAS no.	9028-86-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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.