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Results 1 - 10 of 18 > >>
EC Number Reaction Commentary Reference
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 homogentisate -
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 rate-determining step in catalysis is a protein conformation change 395367
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-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 -, 395373
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 enzyme form 3: ordered bi bi mechanism where 4-hydroxyphenylpyruvate is added prior to oxygen and CO2 released before homogentisate 395383
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 evidence against participation of a quinol as a free intermediate 395385
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 in plants this enzyme activity is involved in two distinct metabolic processes, the biosynthesis of prenylquinones and the catabolism of tyrosine 395398
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 addition of substrate and oxygen to the holoenzyme is formally random, holo-enzym in complex with substrate has a 3600-fold increase in oxygen reactivity 657978
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-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 658030
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 mechanism of oxygen binding and activation, structural relationship to other dioxygenases 658980
Show all pathways known for 1.13.11.27Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.274-hydroxyphenylpyruvate + O2 = homogentisate + CO2 the C-terminal helix forms a gate for substrate access to the active site around a nonheme ferrous iron center 660236
Results 1 - 10 of 18 > >>