Tryptophanase

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 .

References

  • 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.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes

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