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1.13.11.27: 4-hydroxyphenylpyruvate dioxygenase

This is an abbreviated version!
For detailed information about 4-hydroxyphenylpyruvate dioxygenase, go to the full flat file.

Word Map on EC 1.13.11.27

Reaction

4-hydroxyphenylpyruvate
+
O2
=
homogentisate
 +
CO2

Synonyms

4-HPPD, 4-hydroxyphenylpyruvare dioxygenase, 4-hydroxyphenylpyruvate dioxygenase, 4-hydroxyphenylpyruvic acid dioxygenase, 4HPPD, ASJ32_19370, At-HPPD, AtHPPD, AvHPPD-03, EC 1.14.2.2, EC 1.99.1.14, formerly, F Alloantigen, F protein, F-antigen homolog, HPD, hpdA, HPPD, HPPDase, Legiolysin, MsHPPD, oxygenase, 4-hydroxyphenylpyruvate di-, p-hydroxyphenyl pyruvate dioxygenase, p-hydroxyphenylpyruvate dioxygenase, p-hydroxyphenylpyruvate hydroxylase, p-hydroxyphenylpyruvate oxidase, p-hydroxyphenylpyruvic acid hydroxylase, p-hydroxyphenylpyruvic hydroxylase, p-hydroxyphenylpyruvic oxidase, PTO1369, Pt_Hpd, T-cell reactive protein, TF-AG, YS103B

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.27 4-hydroxyphenylpyruvate dioxygenase

Crystallization

Crystallization on EC 1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a ligand-mediated conformational switch in helix H11 mediates rapid substrate access followed by active site closing and efficient product release through H11 opening. In mutant HPPD, large differences in H11 gating are found with correlation to experimentally measured herbicide tolerance
structure in complex with inhibitor 2-benzyl-5-(5-hydroxy-1-methyl-1H-pyrazole-4-carbonyl)-1H-isoindole-1,3(2H)-dione at a resolution of 1.8 A. The two carbonyl groups of 2-benzoylethen-1-ol formed a bidentate chelating interaction with the metal ion, while the isoindoline-1,3-dione moiety formes pronounced pi-pi stacking interactions with Phe381 and Phe424
structure of HPPD in complex with substrate 4-hydroxyphenylpyruvate at a resolution of 2.80 A. 4-Hydroxyphenylpyruvate takes keto rather than enol form inside the HPPD active pocket. Residues Phe424, Asn423, Glu394, Gln307, Asn282, and Ser267 play important roles in substrate binding and catalytic cycle. Residue Gln293 undergoes a rotation upon the HPPA binding and forms H-bond network of Ser267-Asn282-Gln307-Gln293, resulting in the transformation of HPPD from an inactive state to active state
structures in complex with inhibitors nitisinone, sulcotrione and mesotrione. A conformational change of Phe428 is found at the C-terminal alpha-helix in the inhibitor-bound structures and the inhibition kinetics of drugs are related to steric hindrance of Phe428
substrate-free form
-
with and without inhibitors [1-tert-butyl-3-(2,4-dichlorophenyl)-5-hydroxy-1H-pyrazol-4-yl][2-chloro-4-(methylsulfonyl)phenyl]methanone or 1-(1,1-dimethylethyl)-5-hydroxy-4-(3-(4-(methoxy)phenyl)-2-methyl-4-(methylsulfonyl)benzoyl)pyrazole
comparison of Arabidopsis thaiana and human enzyme. In human, the carboxyl group of substrate 4-hydroxyphenylpyruvate interacts by a H-bond network formed by Gln334, metal-binding ligand Glu349, and Asn363 in the C-terminal helix. The 4-hydroxyl group of the substrate interacts with Gln251 and Gln265
homology modeling of structure and docking of inhibitors. Each molecule consists of 9 alpha-helices and 2 twisted barrel-like beta-sheets, and the active site is located at the C-terminus
crystals are grown by sitting-drop vapor diffusion method at 20°C
crystal structure analysis of HPPD-Fe(II)-acetate complex, PDB ID 1CJX
-
crystal structure at 2.4 A resolution
-
hanging-drop method in 18-25% PEG 4000, 0.2 M ammonium acetate, 0.1 M trisodium citrate, pH 5.6, at room temperature
-
with and without inhibitors 1-(1,1-dimethylethyl)-5-hydroxy-4-(3-(4-(methoxy)phenyl)-2-methyl-4-(methylsulfonyl)benzoyl)pyrazole or [1-tert-butyl-3-(2,4-dichlorophenyl)-5-hydroxy-1H-pyrazol-4-yl][2-chloro-4-(methylsulfonyl)phenyl]methanone
Fe(II)-form in complex with inhibitor 2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione
a ligand-mediated conformational switch in helix H11 mediates rapid substrate access followed by active site closing and efficient product release through H11 opening. In mutant HPPD, large differences in H11 gating are found with correlation to experimentally measured herbicide tolerance
-
substrate-free form
-