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	dioxygen reactivity and the common decarboxylation half reaction, and the hydroxylation half reaction, mechanisms, detailed overview	-, 741762	
1.13.11.27	4-hydroxyphenylpyruvate + O2 = homogentisate + CO2	dioxygen reactivity and the common decarboxylation half reaction, and the hydroxylation half reaction, mechanisms, inhibitor-bound crystal structure, PDB ID 1CJX, analysis, detailed overview	741762	
1.13.11.27	4-hydroxyphenylpyruvate + O2 = homogentisate + CO2	direct involvement of the arene oxide intermediate to the reaction mechanism	725432	
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	homogentisate	-	
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	mechanism of oxygen binding and activation, structural relationship to other dioxygenases	658980	
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	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