catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) or glutamate as the amino donors. Histidine, leucine, asparagine, or arginine are also functional amino donors but to a lesser extent. Can also use alpha-ketoglutarate, oxaloacetate and pyruvate as the amino acceptors. 2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate 2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate 4-methylsulfanyl-2-oxobutanoate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-methionine 2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate Inhibited by malate and nitrotyrosine by approximately 20% at the higher concentration. At 100 uM, canaline and carboxymethoxylamine inhibit aminotransferase activity by 35 and 70%, respectively. Addition of 1.0 mM carboxymethoxylamine lead to a complete inhibition of the aminotransferase activity. Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 6/6. Homodimer. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.