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Literature summary for 1.13.11.27 extracted from

  • Borowski, T.; Bassan, A.; Siegbahn, P.E.
    4-Hydroxyphenylpyruvate dioxygenase: a hybrid density functional study of the catalytic reaction mechanism (2004), Biochemistry, 43, 12331-12342.
    View publication on PubMed
Search for more literature for 1.13.11.27

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure at 2.4 A resolution Pseudomonas fluorescens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required for activity, the active-site iron is in the ferric oxidation state and coordinated by the side chains of two histidines and on glutamate Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylpyruvate + O2 Pseudomonas fluorescens
-
 homogentisate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 ternary enzyme-substrate complex is firstly decarboxylated to the iron(II)-peracid intermediate followed by heterolytic cleavage of the O-O bond yielding an iron(IV)-oxospecies. This attacks the aromatic ring in C1 position. The arene oxide has no catalytic relevance Pseudomonas fluorescens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylpyruvate + O2
-
 Pseudomonas fluorescens homogentisate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
4-HPPD
-
 Pseudomonas fluorescens