, a tryptophanase
is an enzyme
the chemical reaction
- L-tryptophan + H2O 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.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
- BURNS RO, DEMOSS RD "Properties of tryptophanase from Escherichia coli". Biochim. Biophys. Acta. 65 233–44.
- Cowell JL, Maser K and DeMoss, RD "Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties". Biochim. Biophys. Acta 315 449–463.
- NEWTON WA, MORINO Y, SNELL EE "PROPERTIES OF CRYSTALLINE TRYPTOPHANASE". J. Biol. Chem. 240 1211–8.
- The CAS registry number for this enzyme class is .
Gene Ontology (GO) codes