Tryptophanase

In enzymology, a tryptophanase (EC number|4.1.99.1) is an enzyme that catalyzes the chemical reaction

:L-tryptophan + H₂O $ightleftharpoons$ 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.

tructural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1AX4, PDB link|2C44, and PDB link|2OQX.

References

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External links

::"The CAS registry number for this enzyme class is CAS registry|9024-00-4."

Gene Ontology (GO) codes