| tryptophanase | |||||||||
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Tryptophanase tetramer, E.Coli
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| Identifiers | |||||||||
| EC no. | 4.1.99.1 | ||||||||
| CAS no. | 9024-00-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction
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]
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]
Media related to Tryptophanase at Wikimedia Commons|
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This EC 4.1 enzyme-related article is a stub. You can help Wikipedia by expanding it. |
