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