Glutamate-prephenate aminotransferase

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In enzymology, a glutamate-prephenate aminotransferase (EC 2.6.1.79) is an enzyme that catalyzes the chemical reaction

L-arogenate + 2-oxoglutarate $\rightleftharpoons$ prephenate + L-glutamate

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

[edit] References

IUBMB entry for 2.6.1.79
BRENDA references for 2.6.1.79 (Recommended.)
PubMed references for 2.6.1.79
PubMed Central references for 2.6.1.79
Google Scholar references for 2.6.1.79
Bonner CA, Jensen RA (1985). "Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris". Arch. Biochem. Biophys. 238: 237–46. PMID 3985619.
Siehl DL, Connelly JA, Conn EE (1986). "Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase". Z. Naturforsch. [C]. 41: 79–86. PMID 2939644.
Bonner C, Jensen R (1987). "Prephenate aminotransferase". Methods. Enzymol. 142: 479–87. PMID 3298985.