2-oxoaldehyde dehydrogenase (NAD+)
2-oxoaldehyde dehydrogenase (NAD) | |||||||||
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Identifiers | |||||||||
EC number | 1.2.1.23 | ||||||||
CAS number | 37250-91-2 | ||||||||
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 / EGO | ||||||||
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In enzymology, a 2-oxoaldehyde dehydrogenase (NAD+) (EC 1.2.1.23) is an enzyme that catalyzes the chemical reaction
- a 2-oxoaldehyde + NAD+ + H2O a 2-oxo acid + NADH + H+
The 3 substrates of this enzyme are 2-oxoaldehyde, NAD+, and H2O, whereas its 3 products are 2-oxo 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 2-oxoaldehyde:NAD+ 2-oxidoreductase. Other names in common use include alpha-ketoaldehyde dehydrogenase, methylglyoxal dehydrogenase, NAD+-linked alpha-ketoaldehyde dehydrogenase, 2-ketoaldehyde dehydrogenase, NAD+-dependent alpha-ketoaldehyde dehydrogenase, and 2-oxoaldehyde dehydrogenase (NAD+). This enzyme participates in pyruvate metabolism.
References
- Monder C (1967). "Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate". J. Biol. Chem. 242 (20): 4603–9. PMID 4383524.
- Ray M, Ray S (1982). "On the interaction of nucleotides and glycolytic intermediates with NAD-linked alpha-ketoaldehyde dehydrogenase". J. Biol. Chem. 257 (18): 10571–4. PMID 7107626.
- Ray S, Ray M (1982). "Purification and characterization of NAD and NADP-linked alpha-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate". J. Biol. Chem. 257 (18): 10566–70. PMID 7107625.