Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis
Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis
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DOI:
10.1128/aem.02456-07
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发表时间:
2008-05-01
影响因子:
4.4
通讯作者:
Gosset, Guillermo
中科院分区:
文献类型:
--
作者:
Chavez-Bejar, Maria I.;Lara, Alvaro R.;Gosset, Guillermo
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.