EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
    4.2.1.51 | -999 |
- |
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 |
684578 |
| 4.2.1.51 | -999 |
- |
Mtr1 mutant of rice indicates accumulation of L-phenylalanine, L-trytophan, and of several phenylpropanoids, suggesting a link between the synthesis of L-phenylalanine and L-trytophan, mtr1-D mutant gene indicates point mutation in the putative allosteric regulatory region, wild-type enzyme is feedback regulated by L-phenylalanine, Mtr1 mutant has reduced feedback activity and accumulates L-phenylalanine, critical for regulating the size of the pool of L-phenylalanine in plant cells |
694629 |
| 4.2.1.51 | -999 |
- |
seasonal clonal variations, and effects of stresses and leaf age on prephenate dehydratase enzyme activity in different tea samples, overview |
714881 |
| 4.2.1.51 | -999 |
- |
substrate specificity of the bifunctional enzyme, activity of mutant enzymes, overview |
649980 |
| 4.2.1.51 | -999 |
- |
three-dimensional enzyme structure, oligomeric state determined, circular dichroism method and bioinformatics tools, hydrodynamic properties, analytical ultracentrifugation experiments, small angle X-ray scattering, enzyme stability shown by molecular dynamics simulations, predicted as a flat disk protein with an asymmetric shape |
695038 |
| 4.2.1.51 | -999 |
- |
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities |
692260 |
| 4.2.1.51 | -999 |
- |
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities, prephenate dehydratase activity spectrophotometric quantified by monitoring the appearance of phenylpyruvate at 320 nm in end-point assays |
692260 |
| 4.2.1.51 | 0.32 |
- |
mutant F185Y, pH 7.5, 30°C |
649516 |
| 4.2.1.51 | 0.39 |
- |
mutant T183S, pH 7.5, 30°C |
649516 |
| 4.2.1.51 | 2.37 |
- |
mutant S99A, pH 7.5, 30°C |
649516 |
