Tryptophan transaminase

tryptophan transaminase
Identifiers
EC number	2.6.1.27
CAS number	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 / EGO
Search PMC articles PubMed articles NCBI proteins

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

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

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.

References

• George H, Gabay S (1968). "Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase". Biochim. Biophys. Acta 167 (3): 555–66. doi:10.1016/0005-2744(68)90045-4. PMID 5722279.
• O'Neil SR, DeMoss RD (1968). "Tryptophan transaminase from Clostridium sporogenes". Arch. Biochem. Biophys. 127 (1): 361–9. doi:10.1016/0003-9861(68)90237-3. PMID 5697992.
• Tangen O, Fonnum F and Haavaldsen R (1965). "Separation and purification of aromatic amino acid transaminases from rat brain". Biochim. Biophys. Acta 96: 82–90. doi:10.1016/0005-2787(65)90612-x. PMID 14285270.