EC Number   |
Title   |
Organism   |
---|
  1.14.14.9 | A single amino acid substitution in aromatic hydroxylase (HpaB) of Escherichia coli alters substrate specificity of the structural isomers of hydroxyphenylacetate |
Escherichia coli |
  1.14.14.9 | A single amino acid substitution in aromatic hydroxylase (HpaB) of Escherichia coli alters substrate specificity of the structural isomers of hydroxyphenylacetate |
Escherichia coli BL21-DE3 |
  1.14.14.9 | A single-site mutation at Ser146 expands the reactivity of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase |
Acinetobacter baumannii |
  1.14.14.9 | Catalytic activity of the two-component flavin-dependent monooxygenase from Pseudomonas aeruginosa toward cinnamic acid derivatives |
Pseudomonas aeruginosa |
  1.14.14.9 | Characterization of enzymatic properties of two novel enzymes, 3,4-dihydroxyphenylacetate dioxygenase and 4-hydroxyphenylacetate 3-hydroxylase, from Sulfobacillus acidophilus TPY |
Sulfobacillus acidophilus |
  1.14.14.9 | Characterization of enzymatic properties of two novel enzymes, 3,4-dihydroxyphenylacetate dioxygenase and 4-hydroxyphenylacetate 3-hydroxylase, from Sulfobacillus acidophilus TPY |
Sulfobacillus acidophilus TPY |
  1.14.14.9 | Control of C4a-hydroperoxyflavin protonation in the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase |
Acinetobacter baumannii |
  1.14.14.9 | De novo biosynthesis of tyrosol acetate and hydroxytyrosol acetate from glucose in engineered Escherichia coli |
Escherichia coli |
  1.14.14.9 | De novo biosynthesis of tyrosol acetate and hydroxytyrosol acetate from glucose in engineered Escherichia coli |
Escherichia coli BL21-DE3 |
  1.14.14.9 | Hydroxylation of 4-hydroxyphenylethylamine derivatives by R263 variants of the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase |
Acinetobacter baumannii |