Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.13.11.27 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)

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Zea mays
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
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

Subunits

Subunits Comment Organism
dimer crystallization data Zea mays
dimer crystallization data Arabidopsis thaliana