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Literature summary extracted from

  • Rundgren, M.
    Some kinetic properties of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P.J. 874 (1983), Eur. J. Biochem., 133, 657-663.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.27 2-hydroxyphenylacetate product inhibition Pseudomonas sp.
1.13.11.27 bathophenanthroline
-
Pseudomonas sp.
1.13.11.27 homogentisate product inhibition Pseudomonas sp.
1.13.11.27 phenylpyruvate non-competitive inhibition with 4-hydroxyphenylpyruvate as substrate Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.27 Pseudomonas sp.
-
-
-
1.13.11.27 Pseudomonas sp. P.J. 874
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 mono-iso-ordered bi-bi mechanism with binding of 4-hydroxyphenylpyruvate before O2 and release of CO2 before homogentisate. A Theorell-Chance mechanism can not be excluded Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.27 4-hydroxyphenylpyruvate + O2
-
Pseudomonas sp. homogentisate + CO2
-
?
1.13.11.27 4-hydroxyphenylpyruvate + O2
-
Pseudomonas sp. P.J. 874 homogentisate + CO2
-
?
1.13.11.27 phenylpyruvate + O2
-
Pseudomonas sp. 2-hydroxyphenylacetate + CO2
-
?
1.13.11.27 phenylpyruvate + O2
-
Pseudomonas sp. P.J. 874 2-hydroxyphenylacetate + CO2
-
?