Indole-3-acetaldehyde reductase (NADH)

Enzyme From Wikipedia, the free encyclopedia

In enzymology, indole-3-acetaldehyde reductase (NADH) (EC 1.1.1.190) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
+ NADH
 

The two substrates of this enzyme are tryptophol and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are indole-3-acetaldehyde, reduced NADH, and a proton.[1][2]

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.

See also

References

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