Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase.

  title={Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase.},
  author={Patrick A. Roche and Thomas John Moorehead and Gordon A. Hamilton},
  journal={Archives of biochemistry and biophysics},
  volume={216 1},
Some kinetic properties of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P.J. 874.
  • M. Rundgren
  • Chemistry, Biology
    European journal of biochemistry
  • 1983
The results conform to a mono-iso-ordered bi-bi mechanism with binding of 4-hydroxyphenylpyruvate before O2 and release of CO2 before homogentisate, and loss of hydrogen at C2 or C6 of the ring of the substrate is thus not the rate-limiting step during the reaction.
Human 4-hydroxyphenylpyruvate dioxygenase. Primary structure and chromosomal localization of the gene.
Results indicate that these proteins are all 4-hydroxyphenylpyruvate dioxygenases, and the identity of the C-terminus makes this part of the molecule a candidate for a functional role in the catalytic process.
Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme.
The primary structure of Pseudomonas 4-hydroxyphenylpyruvate dioxygenase was determined and secondary structure predictions suggest an alpha/beta mixed structure, fairly typical of globular proteins, without long segments of hydrophobicity or charge.
Alternate substrates and inhibitors of bacterial 4-hydroxyphenylpyruvate dioxygenase.
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.
Characterization and subcellular compartmentation of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis in transgenic tobacco.
The molecular and biochemical characterization of an Arabidopsis 4HPPD and the compartmentation of the recombinant protein in chlorophyllous tissues are reported and southern analysis strongly suggested that this 4HP PD is encoded by a single-copy gene.
The Crystal Structures of Zea mays and Arabidopsis 4-Hydroxyphenylpyruvate Dioxygenase
The first x-ray structures of the plant HPPDs of Zea mays and Arabidopsis in their substrate-free form are reported, providing direct evidence that the C-terminal helix gates substrate access to the active site around a nonheme ferrous iron center.
p-Hydroxyphenylpyruvate dioxygenase inhibitor-resistant plants.
A third strategy of resistance based on the increase of p-hydroxyphenylpyruvate substrate flux has been developed and a high level of herbicide resistance was observed in leaves of the transgenic HPPD-PDH plants.
The Mode of Action of Isoxaflutole II. Characterization of the Inhibition of Carrot 4-Hydroxyphenylpyruvate Dioxygenase by the Diketonitrile Derivative of Isoxaflutole☆☆☆
Abstract Isoxaflutole (5-cyclopropylisoxazol-4-yl 2-mesyl-4-trifluromethylphenyl ketone) is a novel herbicide for broadleaf and grass weed control in corn and sugarcane which acts by inhibiting the
Tyrosinaemia type III: Immunochemical studies on 4-hydroxyphenylpyruvic acid dioxygenase and molecular cloning of cDNA for the enzyme
To better comprehend structure-function relationships, gene organization and biosynthetic regulatory mechanisms, the 4HPA dioxygenase gene is of interest with regard to type I tyrosineemia and type III tyrosinaemia.
Tocopherol biosynthesis: chemistry, regulation and effects of environmental factors
Tocopherols are lipophilic antioxidants and together with tocotrienols belong to the vitamin-E family. The four forms of tocopherols (α-, β-, γ- and δ-tocopherols) consist of a polar chromanol ring


Purification of p-hydroxyphenylpyruvate hydroxylase from rat liver--requirement for cofactors.
The enzyme p-hydroxyphenylpyruvate hydroxylase (EC from rat liver was studied with the assay method which measures the release of 14CO2 from p-HydroxYPhenyl [carboxy-14C]pyruVate, and appears to be different from those described by other workers from the liver of dog, human, chicken, and frog.
Multiple forms of human 4-hydroxyphenylpyruvate dioxygenase (II).
  • M. Rundgren
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1977
Radiochemical assays for p-hydroxyphenylpyruvate hydroxylase activity in human liver.
  • B. Lindblad
  • Chemistry
    Clinica chimica acta; international journal of clinical chemistry
  • 1971
Studies on a possible reaction intermediate of p-hydroxyphenylpyruvate dioxygenase.
The oxidation in liver of l-tyrosine to acetoacetate through p-hydroxyphenylpyruvate and homogentisic acid.
A more active L-tyrosine oxidation system than any hitherto used, freed from other reactions occurring in crude liver homogenates, was needed to investigate these discrepancies.
Effects of the luxoid gene (lu) on liver esterase isozymes of the mouse.
A system was devised to compare the distribution of non-specific esterases in the tissues of animals whose phenotypes are manifestations of alternative alleles at a single locus and the results are presented more fully here.
The gel-filtration behaviour of proteins related to their molecular weights over a wide range.
1. Correlation between elution volume, V(e), and molecular weight was investigated for gel filtration of proteins of molecular weights ranging from 3500 (glucagon) to 820000 (alpha-crystallin) on