Tryptophanase

tryptophanase
Tryptophanase tetramer, E.Coli
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a tryptophanase (EC 4.1.99.1) is an enzyme that catalyzes the chemical reaction

L-tryptophan + H₂O ${\displaystyle \rightleftharpoons }$ 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.

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[]

• BURNS RO, DEMOSS RD (1962). "Properties of tryptophanase from Escherichia coli". Biochim. Biophys. Acta. 65 (2): 233–44. doi:10.1016/0006-3002(62)91042-9. PMID 14017164.
• Cowell JL, Maser K, DeMoss, RD (1973). "Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties". Biochim. Biophys. Acta. 315: 449–463. doi:10.1016/0005-2744(73)90276-3.
• NEWTON WA, MORINO Y, SNELL EE (1965). "Properties of Crystalline Tryptophanase". J. Biol. Chem. 240: 1211–8. PMID 14284727.

External links[]

• Media related to Tryptophanase at Wikimedia Commons