EC Number   |
Reaction |
Reference |
|---|
    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 |
reaction mechanism, overview |
724325, 724392 |
| 1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 |
reaction mechanism, quantum and molecular mechanics (QM/MM) combined with coupling techniques and molecular dynamics, overview |
743211 |
| 1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 |
reaction mechanism, quantum mechanics/molecular mechanics calculations and simulations, detailed overview |
-, 742742 |
| 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 |
the C-terminal helix forms a gate for substrate access to the active site around a nonheme ferrous iron center |
660236 |
| 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, completely sequestering the active site from solvent |
660236 |
| 1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 |
The data of the rapid acid quench followd by HPLC product analysis, indicate that the homogenisate product is formed during one turnover, as the amount of product is equivalent to the enzyme-substrate complex at 191 ms. |
672033 |
