Tryptophanase Explained

tryptophanase
Ec Number:	4.1.99.1
Cas Number:	9024-00-4
Go Code:	0009034
Width:	270

The enzyme tryptophanase catalyzes the chemical reaction

L-tryptophan + H₂O

\rightleftharpoons indole + pyruvate + 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] [2] [3]}

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1AX4,^[4] 2C44,^[5] and 2OQX.^[6]

Notes and References

1. BURNS RO, DEMOSS RD . 1962 . Properties of tryptophanase from Escherichia coli . Biochim. Biophys. Acta . 65 . 233 - 44 . 14017164 . 10.1016/0006-3002(62)91042-9 . 2 .
2. Cowell JL, Maser K, DeMoss, RD . 1973 . Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties . . 315 . 449 - 463 . 10.1016/0005-2744(73)90276-3.
3. NEWTON WA, MORINO Y, SNELL EE . Properties of Crystalline Tryptophanase . 1965 . J. Biol. Chem. . 240 . 3 . 1211 - 8 . 10.1016/S0021-9258(18)97562-9 . 14284727 . free .
4. Retrieved from Protein Data Bank (PDB)
5. Retrieved from Protein Data Bank (PDB)
6. Retrieved from Protein Data Bank (PDB)