Tryptophan Dehydrogenase

In enzymology, a tryptophan dehydrogenase (EC 1.4.1.19) is an enzyme that catalyzes the chemical reaction

L-tryptophan + NAD(P)+ + H2O (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+

The 4 substrates of this enzyme are L-tryptophan, NAD+, NADP+, and H2O, whereas its 5 products are (indol-3-yl)pyruvate, NH3, NADH, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-tryptophan:NAD(P)+ oxidoreductase (deaminating). Other names in common use include NAD(P)+-L-tryptophan dehydrogenase, L-tryptophan dehydrogenase, L-Trp-dehydrogenase, and TDH. This enzyme has at least one effector, calcium.

Other articles related to "tryptophan":

Amino Acid Synthesis - Amino Acid Biosynthesis Is Regulated By Feedback Inhibition - Additional Regulation Based On Amino Acid Families - Erythrose 4-phosphate and Phosphoenolpyruvate Family
... Phenylalanine, tyrosine, and tryptophan are known as the aromatic amino acids ... its synthesis regulated from tyrosine, phenylalanine, and tryptophan, respectively ... to the final end product, either tyrosine, phenylalanine, or tryptophan ...