Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 74, Issue 10, Pages 3284-3290Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.02456-07
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The expression of the feedback inhibition-insensitive enzyme cyclohexadienyl dehydrogenase (TyrC) from Zymomonas mobilis and the chorismate mutase domain from native chorismate mutase-prephenate dehydratase (PheA(CM)) from Escherichia coli was compared to the expression of native feedback inhibition-sensitive chorismate mutase-prephenate dehydrogenase (CM-TyrA(P)) with regard to the capacity to produce L-tyrosine in E. coli strains modified to increase the carbon flow to chorismate. Shake flask experiments showed that TyrC increased the yield of L-tyrosine from glucose (YL-Tyr/Glc) by 6.8-fold compared to the yield obtained with CM-TyrA(P). In bioreactor experiments, a strain expressing both TyrC and PheA(CM) produced 3 g/liter of L-tyrosine with a YL-Tyr/Glc of 66 mg/g. These values are 46 and 48% higher than the values for a strain expressing only TyrC. The results show that the feedback inhibition-insensitive enzymes can be employed for strain development as part of a metabolic engineering strategy for L-tyrosine production.
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