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Literature summary for 1.14.14.9 extracted from

  • Arunachalam, U.; Massey, V.; Miller, S.M.
    Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme (1994), J. Biol. Chem., 269, 150-155.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Br- retards the oxidative half-reaction Pseudomonas putida
Cl- retards the oxidative half-reaction Pseudomonas putida
F- retards the oxidative half-reaction Pseudomonas putida
I- retards the oxidative half-reaction Pseudomonas putida
N3- retards the oxidative half-reaction Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylacetate + NADH + O2 Pseudomonas putida
-
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas putida

Reaction

Reaction Comment Organism Reaction ID
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O two-protein enzyme: the flavoprotein catalyzes the non-productive oxidation of NADH without substrate hydroxylation and the coupling protein is an absolute requirement for productive hydroxylation. Reaction mechanism and formation of 3 flavin-oxygen intermediates are studied Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-(4-hydroxyphenyl)propionate + ?
-
Pseudomonas putida 3-(3,4-dihydroxy)phenylpropionate + ?
-
?
4-aminophenylacetate + ?
-
Pseudomonas putida 4-amino-3-hydroxyphenylacetate + ?
-
?
4-hydroxyphenylacetate + NADH + O2
-
Pseudomonas putida 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein monooxygenase, absolute requirement Pseudomonas putida