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Literature summary for 4.2.1.51 extracted from

  • Chavez-Bejar, M.I.; Lara, A.R.; Lopez, H.; Hernandez-Chavez, G.; Martinez, A.; Ramirez, O.T.; Bolivar, F.; Gosset, G.
    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 (2008), Appl. Environ. Microbiol., 74, 3284-3290.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli, PB12 strain, pCR-BluntII-TOPO, additional strains and plasmids listed Zymomonas mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis Q5NLV8 encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
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Zymomonas mobilis ATCC 31821 Q5NLV8 encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 comparison of prephenate dehydratase isolated from Zymomonas mobilis to those of Escherichia coli with regard to the capacity to produce L-tyrosine in Escherichia coli strains modified to increase the carbon flow to chorismate, kinetic and stoichiometric parameters determined in shake flask experiments, parameters determined from data generated in bioreactor experiments, possibility to employ feedback inhibition-insensitive enzymes for strain development as part of a metabolic engineering strategy for L-tyrosine production Zymomonas mobilis