View source for D-amino-acid transaminase

{{enzyme
| Name = Glutamate-prephenate aminotransferase
| EC_number = 2.6.1.79
| CAS_number = 
| IUBMB_EC_number = 2/6/1/79
| GO_code = 
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''glutamate-prephenate aminotransferase''' ({{EC number|2.6.1.79}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:L-arogenate + 2-oxoglutarate <math>\rightleftharpoons</math> prephenate + L-glutamate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[L-arogenate]] and [[2-oxoglutarate]], whereas its two [[product (chemistry)|products]] are [[prephenate]] 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-arogenate:2-oxoglutarate aminotransferase'''. Other names in common use include '''prephenate transaminase (ambiguous)''', '''PAT (ambiguous)''', and '''L-glutamate:prephenate aminotransferase'''.

==References==
{{reflist|1}}
* {{cite journal | author = Bonner CA, Jensen RA | year = 1985 | title = Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris | journal = Arch. Biochem. Biophys.  | volume = 238 | pages = 237&ndash;46  | pmid = 3985619 | doi = 10.1016/0003-9861(85)90161-4 | issue = 1 }}
* {{cite journal | author = Siehl DL, Connelly JA, Conn EE | year = 1986 | title = Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase | journal = Z. Naturforsch. [C].  | volume = 41 | pages = 79&ndash;86  | pmid = 2939644 | issue = 1-2 }}
* {{cite journal | author = Bonner C, Jensen R | year = 1987 | title = Prephenate aminotransferase | journal = Methods Enzymol.  | volume = 142 | pages = 479&ndash;87  | pmid = 3298985 | doi = 10.1016/S0076-6879(87)42059-4 }}

{{DEFAULTSORT:Glutamate-prephenate aminotransferase}}
[[Category:EC 2.6.1]]
[[Category:Enzymes of unknown structure]]


{{transferase-stub}}