4-Hydroxyphenylpyruvate dioxygenase.

@article{Moran20054HydroxyphenylpyruvateD,
  title={4-Hydroxyphenylpyruvate dioxygenase.},
  author={Graham R. Moran},
  journal={Archives of biochemistry and biophysics},
  year={2005},
  volume={433 1},
  pages={
          117-28
        }
}
  • G. Moran
  • Published 2005
  • Biology, Chemistry
  • Archives of biochemistry and biophysics
Mechanism of benzylic hydroxylation by 4-hydroxymandelate synthase. A computational study.
TLDR
This study focuses on the part of the HMS catalytic cycle that starts from the oxoferryl intermediate and finds that the conformation of the Ser201 side chain in the second coordination shell has a key role in directing the reaction of Fe(IV)═O into either the HMS or the HPPD channel.
The different catalytic roles of the metal-binding ligands in human 4-hydroxyphenylpyruvate dioxygenase.
TLDR
Modelling the rearrangement of the co-ordination environment and the dynamic behaviour of bound dioxygen in the H266A and H183A variants suggest that the residues regulate the geometry of the reactive oxygen intermediate during the oxidation reaction.
Role of the N-terminus in human 4-hydroxyphenylpyruvate dioxygenase activity.
TLDR
It is demonstrated that the N-terminus maintains the stability of the domain interface to allow for catalysis at the active site of HPPD, a key enzyme in tyrosine catabolism.
Structural and functional characterization of 4-hydroxyphenylpyruvate dioxygenase from the thermoacidophilic archaeon Picrophilus torridus
TLDR
The biochemical characterization of an Hpd from the extremophilic archaeon Picrophilustorridus is reported, together with its three-dimensional structure at a resolution of 2.6 Å, showing that the enzyme is protected in vivo from denaturation and/or is only partially adapted to the harsh environmental conditions in the cytosol of P. torridus.
4-Hydroxyphenylglycine biosynthesis in Herpetosiphon aurantiacus: a case of gene duplication and catalytic divergence
TLDR
This study confirmed the capability of H. aurantiacus for HPG production and reported a comprehensive analysis on the phylogeny of these enzymes, which sheds light on the evolution of paralogous gene sets and the ensuing metabolic diversity in a barely studied bacterium.
Role of substrate positioning in the catalytic reaction of 4-hydroxyphenylpyruvate dioxygenase-A QM/MM Study.
TLDR
From the computed reaction free energy profiles it follows that the most likely mechanism of 4-hydroxyphenylpyruvate dioxygenase involves electrophilic attack on the C1 carbon of the ring and subsequent single-step heterolytic migration of the substituent.
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References

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(4-Hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis: the basis for ordered substrate addition.
TLDR
The binding of ligands to HPPD from Streptomyces avermitilis is examined and data show that HPP binds to the apoenzyme and that the apo-HPPD does not bind Fe(II) to generate active holoenzyme.
Engineering p-hydroxyphenylpyruvate dioxygenase to a p-hydroxymandelate synthase and evidence for the proposed benzene oxide intermediate in homogentisate formation.
TLDR
High-resolution HPLC assay analysis of each His6-tagged mutant indicated that F337I successfully produced p-hydroxymandelate, along with homogentisate and an unknown compound, which was determined to be an oxepinone derived from the benzene-oxide intermediate long hypothesized in HPD catalysis.
Alternate substrates and inhibitors of bacterial 4-hydroxyphenylpyruvate dioxygenase.
TLDR
Two substrate analogues of 4-hydroxyphenylpyruvate dioxygenase proved to be alternate substrates for the enzyme, and the implications of these results with regard to the catalytic mechanism are discussed.
Inhibition of p-hydroxyphenylpyruvate dioxygenase by the diketonitrile of isoxaflutole: a case of half-site reactivity.
TLDR
It is reported for the first time on the purification to homogeneity of a plant enzyme, as obtained from recombinant Escherichia coli cells expressing a cDNA encoding carrot HPPD, that exerts a slow and tight-binding inhibition of HPPD.
Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
TLDR
The reactions catalyzed by this superfamily of enzymes are described, key active site features revealed by structural studies are highlighted, and results from spectroscopic and other approaches that provide insights into the chemical mechanisms are summarized.
Interaction of (4-hydroxyphenyl)pyruvate dioxygenase with the specific inhibitor 2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione.
TLDR
It is proposed that the bidentate association of NTBC with the active site metal ion precedes the Lewis acid-assisted conversion of the bound enol to the enolate to form the oxidized holoenzyme, the HPPD.Fe(II).
Structure of the ferrous form of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis in complex with the therapeutic herbicide, NTBC.
TLDR
The three-dimensional structure of the Fe(II) form of HPPD from Streptomyces avermitilis in complex with the inhibitor 2-nitro-4-(triflouromethyl)benzoyl]-1,3-cyclohexanedione (NTBC) has been determined and is suggestive of a binding mode for the substrate and/or a transition state, which may be the origin of the exceedingly high affinity these inhibitors have for HPPD.
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase
Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of clavulanic acid, a clinically used inhibitor of serine
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