Tryptophan transaminase

In enzymology, a tryptophan transaminase (EC 2.6.1.27) is an enzyme that catalyzes the chemical reaction

L-tryptophan + 2-oxoglutarate ${\displaystyle \rightleftharpoons }$ (indol-3-yl)pyruvate + L-glutamate

tryptophan transaminase
L-tryptophan aminotransferase dimer, Arabidopsis thaliana
Identifiers
EC no.	2.6.1.27
CAS no.	9022-98-4
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

Thus, the two substrates of this enzyme are L-tryptophan and 2-oxoglutarate, whereas its two products are (indol-3-yl)pyruvate and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-tryptophan:2-oxoglutarate aminotransferase. Other names in common use include L-phenylalanine-2-oxoglutarate aminotransferase, tryptophan aminotransferase, 5-hydroxytryptophan-ketoglutaric transaminase, hydroxytryptophan aminotransferase, L-tryptophan aminotransferase, and L-tryptophan transaminase. This enzyme participates in tryptophan metabolism. It employs one cofactor, pyridoxal phosphate.