Tryptophanase

From Wikipedia, the free encyclopedia

In enzymology, a tryptophanase (EC 4.1.99.1) 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 4.1.99.1
BRENDA references for 4.1.99.1 (Recommended.)
PubMed references for 4.1.99.1
PubMed Central references for 4.1.99.1
Google Scholar references for 4.1.99.1
BURNS RO, DEMOSS RD (1962). "Properties of tryptophanase from Escherichia coli". Biochim. Biophys. Acta. 65: 233–44. doi:10.1016/0006-3002(62)91042-9. PMID 14017164.
Cowell JL, Maser K and DeMoss, RD (1973). "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 (1965). "PROPERTIES OF CRYSTALLINE TRYPTOPHANASE". J. Biol. Chem. 240: 1211–8. PMID 14284727.