Tryptophanase

In enzymology, a tryptophanase is an enzyme that catalyzes the chemical reaction


 * L-tryptophan + H2O $$\rightleftharpoons$$ indole + pyruvate + NH3

Thus, the two substrates of this enzyme are L-tryptophan and H2O, whereas its 3 products are indole, pyruvate, and NH3.

This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tryptophan indole-lyase (deaminating; pyruvate-forming). Other names in common use include L-tryptophanase, and L-tryptophan indole-lyase (deaminating). This enzyme participates in tryptophan metabolism and nitrogen metabolism. It has 2 cofactors: pyridoxal phosphate, and Potassium.

Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes, , and.