- Source: Dihydroxyphenylalanine transaminase
In enzymology, a dihydroxyphenylalanine transaminase (EC 2.6.1.49) is an enzyme that catalyzes the chemical reaction
3,4-dihydroxy-L-phenylalanine + 2-oxoglutarate
⇌
{\displaystyle \rightleftharpoons }
3,4-dihydroxyphenylpyruvate + L-glutamate
Thus, the two substrates of this enzyme are 3,4-dihydroxy-L-phenylalanine and 2-oxoglutarate, whereas its two products are 3,4-dihydroxyphenylpyruvate 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 3,4-dihydroxy-L-phenylalanine:2-oxoglutarate aminotransferase. Other names in common use include dopa transaminase, dihydroxyphenylalanine aminotransferase, aspartate-DOPP transaminase (ADT), L-dopa transaminase, dopa aminotransferase, glutamate-DOPP transaminase (GDT), phenylalanine-DOPP transaminase (PDT), DOPA 2-oxoglutarate aminotransferase, and DOPAATS. This enzyme participates in tyrosine metabolism. It employs one cofactor, pyridoxal phosphate.
References
Fonnum F, Larsen K (1965). "Purification and properties of dihydroxyphenylalanine transaminase from guinea pig brain". J. Neurochem. 12 (7): 589–98. doi:10.1111/j.1471-4159.1965.tb04251.x. PMID 5829872.
