Acyltransferase that catalyzes the formation of methyl anthranilate, a compound implicated in the 'foxy' odor character of Concord grapes. Can use a variety of alcohol substrates when assayed with both benzoyl-CoA and anthraniloyl-CoA. anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate benzoyl-CoA + benzyl alcohol = benzyl benzoate + CoA K(+), Ca(2+), Mg(2+) and Mn(2+) increase enzyme activity while Cu(2+) and Zn(2+) inactivate the enzyme. kcat is 0.045 sec(-1) with benzoyl-CoA as substrate (with native enzyme). kcat is 0.022 sec(-1) with anthraniloyl-CoA as substrate (with native enzyme). kcat is 0.0035 sec(-1) with methanol as substrate (with native enzyme). kcat is 0.045 sec(-1) with benzoyl-CoA as substrate (with recombinant enzyme). kcat is 0.01 sec(-1) with anthraniloyl-CoA as substrate (with recombinant enzyme). kcat is 0.0058 sec(-1) with methanol as substrate (with recombinant enzyme). Optimum pH is 7.0-9.0. Monomer. Expressed in berry outer mesocarp, but not in berry skin. Expression starts when the berries began to change the color. It increases throughout berry development to reach a maximum level in very mature berries. No AMAT activity can be detected in Vitis vinifera grapes. Belongs to the plant acyltransferase family.