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Literature summary extracted from

  • Arunachalam, U.; Massey, V.
    Studies on the oxidative half-reaction of p-hydroxyphenylacetate 3-hydroxylase (1994), J. Biol. Chem., 269, 11795-11801.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.9 4-hydroxyphenylacetate substrate inhibition by concentrations greater than 0.1 mM Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.9 Pseudomonas putida
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.9 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O dehydration of the C4a-hydroxyflavin is the rate-determining step in catalysis Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.9 2,4-dihydroxybenzoate
-
Pseudomonas putida ?
-
?
1.14.14.9 3-(4-hydroxyphenyl)propionate + ?
-
Pseudomonas putida 3-(3,4-dihydroxy)phenylpropionate + ?
-
?
1.14.14.9 4-aminobenzoate + ?
-
Pseudomonas putida 4-amino-3-hydroxybenzoate + ?
-
?
1.14.14.9 4-aminophenylacetate + ?
-
Pseudomonas putida 4-amino-3-hydroxyphenylacetate + ?
-
?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2
-
Pseudomonas putida 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
1.14.14.9 additional information substrates become hydroxylated at a position ortho to the hydroxyl group, 4-chlorophenylacetate, 4-fluorobenzoate and benzoate are not hydroxylated Pseudomonas putida ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.14.9 0.833
-
4-hydroxyphenylacetate
-
Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.9 NADH
-
Pseudomonas putida