Indole-3-acetaldehyde reductase (NADH)
indole-3-acetaldehyde reductase (NADH) | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.190 | ||||||||
CAS no. | 58875-06-2 | ||||||||
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 / QuickGO | ||||||||
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In enzymology, an indole-3-acetaldehyde reductase (NADH) (EC 1.1.1.190) is an enzyme that catalyzes the chemical reaction
- (indol-3-yl)ethanol + NAD+ (indol-3-yl)acetaldehyde + NADH + H+
Thus, the two substrates of this enzyme are (indol-3-yl)ethanol and NAD+, whereas its 3 products are , NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (indol-3-yl)ethanol:NAD+ oxidoreductase. Other names in common use include indoleacetaldehyde reductase, indole-3-acetaldehyde reductase (NADH), and indole-3-ethanol:NAD+ oxidoreductase. This enzyme participates in tryptophan metabolism.
References[]
- Brown HM, Purves WK (1976). "Isolation and characterization of indole-3-acetaldehyde reductases from Cucumis sativus". J. Biol. Chem. 251 (4): 907–13. PMID 2607.
Categories:
- EC 1.1.1
- NADH-dependent enzymes
- Enzymes of unknown structure
- EC 1.1.1 stubs