Aspartyl transferase is able to catalyse the PLP dependent transamination reaction between aspartate and 2-oxoglutarate, forming oxaloacetate and glutamate. It is part of the family of PLP dependent amino acid transferase enzymes which have high sequence homology and identical active site organisation, with the only difference being in the amino acid and ketoacid substrates. The enzymes all play key roles in the catabolism of amino acids as the products feed into the Krebs cycle and the Urea cycle.
Defined by 3 residues: TRP:A-130 [auth A-142]ASP:A-211 [auth A-223]LYS:A-246 [auth A-258]