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{{enzyme
| Name = tryptophan transaminase
| EC_number = 2.6.1.27
| CAS_number = 9022-98-4
| IUBMB_EC_number = 2/6/1/27
| GO_code = 0050362
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''tryptophan transaminase''' ({{EC number|2.6.1.27}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:L-tryptophan + 2-oxoglutarate <math>\rightleftharpoons</math> (indol-3-yl)pyruvate + L-glutamate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[L-tryptophan]] and [[2-oxoglutarate]], whereas its two [[product (chemistry)|products]] are [[(indol-3-yl)pyruvate]] and [[L-glutamate]].

This enzyme belongs to the family of [[transferase]]s, 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 (biochemistry)|cofactor]], [[pyridoxal phosphate]].

==References==
{{reflist|1}}
* {{cite journal | author = George H, Gabay S | year = 1968 | title = Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase | journal = Biochim. Biophys. Acta.  | volume = 167 | pages = 555&ndash;66  | pmid = 5722279 | issue = 3 }}
* {{cite journal | author = O'Neil SR, DeMoss RD | year = 1968 | title = Tryptophan transaminase from Clostridium sporogenes | journal = Arch. Biochem. Biophys.  | volume = 127 | pages = 361&ndash;9  | pmid = 5697992 | doi = 10.1016/0003-9861(68)90237-3 | issue = 1 }}
* {{cite journal | author = Tangen O, Fonnum F and Haavaldsen R | year = 1965 | title = Separation and purification of aromatic amino acid transaminases from rat brain | journal = Biochim. Biophys. Acta  | volume = 96 | pages = 82&ndash;90 | pmid=14285270}}

[[Category:EC 2.6.1]]
[[Category:Pyridoxal phosphate enzymes]]
[[Category:Enzymes of unknown structure]]


{{transferase-stub}}