L-tyrosine is an aromatic amino acid with several applications, including its use as a precursor in the synthesis of some drugs, polymers and phenylpropanoids. The general strategy followed for developing microbial strains for the biotechnological production of this amino acid involves the generation of feedback insensitive mutant versions of key enzymes in the common aromatic and the specific L-tyrosine biosynthetic pathways. In this work, the expression of the feedback insensitive cyclohexadienyl dehydrogenase (TyrC) from Zymomonas mobilis and the chorismate mutase domain from native P-protein (PheA_CM) from Escherichia coli was explored as an approach for engineering L-tyrosine production strains. The effects on L-tyrosine production capacity of expressing genes encoding these enzymes was compared to expression of native feedback sensitive chorismate mutase/prephenate dehydrogenase (CM/TyrA_p) in E. coli strains modified to increase carbon flow to chorismate. In shake flasks experiments using minimal medium supplemented with glucose, it was found that TyrC expression increased by 6.8-fold the L-tyrosine yield from glucose, when compared to CM/TyrA_p. In experiments performed with complex medium in a 1-liter bioreactor, strains expressing TyrC or both TyrC and PheA_CM produced L-tyrosine titers of 2 and 3 g/L in 21 and 27 hours, respectively. These results show that simultaneous expression of these two feedback insensitive enzymes can be employed as part of a metabolic engineering strategy for microbial L-tyrosine production.