Multi enzyme coupled catalysis is one of the important methods in the enzymatic preparation of chiral drug intermediates. In this study, the ammonia of L-aspartic acid was transferred to the phenylpyruvic acid, and L-phenylalanine with byproduct pyruvic acid were synthesized by aspartate aminotransferase (AspAT) whole cell. Then, L-tyrosine was enzymatic synthesized when substrate phenol and tyrosine phenol-lyase (TPL) whole cell were added into the reaction system. Some factors affecting dual enzymatic catalysis were investigated. The optimal conditions were 40oC, pH 8.5, 25 g/L of phenylpyruvic acid (PPA), n (PPA): n (L-Asp)=1:1.2, m (AspAT): m (TPL)=1:1, 4 mmol/L of PLP, 0.1 g/L of Tween 80. 30 g/L of ammonium chloride had a promoting effect on dual enzyme coupled catalysis reaction. The method biological synthesis of L-tyrosine with coupled dual enzyme in dual host, not only makes full use of the by-product of the reaction pyruvic acid for higher value-added products, but has reference significance for the reasonable utilization of resources and green synthesis process.