EC Number |
Reaction |
Reference |
---|
1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 |
homogentisate |
- |
1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 |
rate-determining step in catalysis is a protein conformation change |
395367 |
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 |
-, 395373 |
1.13.11.27 | 4-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 |
1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 |
evidence against participation of a quinol as a free intermediate |
395385 |
1.13.11.27 | 4-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 |
1.13.11.27 | 4-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 |
1.13.11.27 | 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 |
658030 |
1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 |
mechanism of oxygen binding and activation, structural relationship to other dioxygenases |
658980 |
1.13.11.27 | 4-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 |