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Literature summary extracted from

  • Fritze, I.M.; Linden, L.; Freigang, J.; Auerbach, G.; Huber, R.; Steinbacher, S.
    The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase (2004), Plant Physiol., 134, 1388-1400.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.27 substrate-free form Zea mays
1.13.11.27 substrate-free form Arabidopsis thaliana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.27 Iron nonheme ferrous iron Zea mays
1.13.11.27 Iron nonheme ferrous iron Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.27 Arabidopsis thaliana
-
-
-
1.13.11.27 Zea mays
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
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 Arabidopsis thaliana
a
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 Zea mays
a

Subunits

EC Number Subunits Comment Organism
1.13.11.27 dimer crystallization data Zea mays
1.13.11.27 dimer crystallization data Arabidopsis thaliana