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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
Author(s) -
María I. Chávez-Béjar,
Alvaro R. Lara,
H. MEJIA LOPEZ,
Georgina HernándezChávez,
Alfredo Martı́nez,
Octavio T. Ramı́rez,
Francisco Bolívar,
Guillermo Gosset
Publication year - 2008
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.02456-07
Subject(s) - chorismate mutase , escherichia coli , metabolic engineering , biology , biochemistry , mutase , gene , tyrosine , phosphoglycerate mutase , microbiology and biotechnology , enzyme , biosynthesis , glycolysis
The expression of the feedback inhibition-insensitive enzyme cyclohexadienyl dehydrogenase (TyrC) fromZymomonas mobilis and the chorismate mutase domain from native chorismate mutase-prephenate dehydratase (PheACM ) fromEscherichia coli was compared to the expression of native feedback inhibition-sensitive chorismate mutase-prephenate dehydrogenase (CM-TyrAp ) with regard to the capacity to producel -tyrosine inE. coli strains modified to increase the carbon flow to chorismate. Shake flask experiments showed that TyrC increased the yield ofl -tyrosine from glucose (Yl -Tyr/Glc) by 6.8-fold compared to the yield obtained with CM-TyrAp . In bioreactor experiments, a strain expressing both TyrC and PheACM produced 3 g/liter ofl -tyrosine with aYl -Tyr/Glcof 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 forl -tyrosine production.

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