Trisha Shetty (Editor)

Tryptophanase

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EC number
  
4.1.99.1

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
9024-00-4

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

Tryptophanase

In enzymology, a tryptophanase (EC 4.1.99.1) is an enzyme that catalyzes 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.

Structural studies

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

References

Tryptophanase Wikipedia