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Tryptophanase

Enzyme that converts tryptophan into indole From Wikipedia, the free encyclopedia

Tryptophanase
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The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

L-tryptophan + H2O indole + pyruvate + NH3
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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]

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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]

References

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