Purification and properties of avian liver p-hydroxyphenylpyruvate hydroxylase.

Wada, Goro; Fellman, J.H.; Fujita, T.S.; Roth, Esther

doi:10.1016/s0021-9258(19)40992-7

Cited by 47 publications

(19 citation statements)

References 27 publications

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“…Another fundamental difference among HPPD structures is that bacterial HPPDs function as tetramers, whereas plant and mammalian HPPDs function as dimers, respectively. 27,28,32 To understand the HPPD chemistry, 3D structures have considerably served the computational studies in the process of herbicide design. Interestingly, the corresponding predictions mostly correlate with experimental data and hence provide valuable insights into how substrate and inhibitor compete for the active site.…”

Section: ■ the Biological Role Of Hppdmentioning

confidence: 99%

“…16,33 This assumption was confirmed in AtHPPD where conserved residues (Asn261 and Ser246) properly orient the HPPA intermediate for the Fe(IV)−oxene electrophilic attack at the aromatic C1. 7,28,38 However, clear functions of individual residues and the means by which the enzymes orchestrate the catalytic cycles are largely unknown. 16 Fe(IV)−Oxene Electrophilic Attack at the Aromatic Ring.…”

Section: ■ the Catalytic Mechanismmentioning

confidence: 99%

“…With a subunit mass between 36 and 50 kDa, − HPPD has a primary structure that comprises two major domains: the flexible N -terminus and the conserved C -terminus that contains the active site. − In plants, the extension of at least 30 residues contributes to a substantial irregularity at the N -terminus with respect to mammalian and bacterial enzymes . A remarkable distinction in plant HPPDs is the inclusion in the last half of the primary structure of a supplementary disordered 15-residue segment close to comparatively unvarying C -terminus. ,, This segment, whose removal is associated with the reduction of the reaction speed without affecting the substrate binding, has been observed to adopt multiple conformations in the presence or absence of ligands .…”

Section: The Structure Of Hppdmentioning

confidence: 99%

“…However, the location of the residues engaged in the facial triad is dependent on the source of HPPD. Another fundamental difference among HPPD structures is that bacterial HPPDs function as tetramers, whereas plant and mammalian HPPDs function as dimers, respectively. ,, …”

Section: The Structure Of Hppdmentioning

confidence: 99%

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4-Hydroxyphenylpyruvate Dioxygenase Inhibitors: From Chemical Biology to Agrochemicals

Ndikuryayo

Moosavi

Yang

et al. 2017

J. Agric. Food Chem.

106

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The development of new herbicides is receiving considerable attention to control weed biotypes resistant to current herbicides. Consequently, new enzymes are always desired as targets for herbicide discovery. 4-Hydroxyphenylpyruvate dioxygenase (HPPD, EC 1.13.11.27) is an enzyme engaged in photosynthetic activity and catalyzes the transformation of 4-hydroxyphenylpyruvic acid (HPPA) into homogentisic acid (HGA). HPPD inhibitors constitute a promising area of discovery and development of innovative herbicides with some advantages, including excellent crop selectivity, low application rates, and broad-spectrum weed control. HPPD inhibitors have been investigated for agrochemical interests, and some of them have already been commercialized as herbicides. In this review, we mainly focus on the chemical biology of HPPD, discovery of new potential inhibitors, and strategies for engineering transgenic crops resistant to current HPPD-inhibiting herbicides. The conclusion raises some relevant gaps for future research directions.

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Section: ■ the Biological Role Of Hppdmentioning

confidence: 99%

Section: ■ the Catalytic Mechanismmentioning

confidence: 99%

Section: The Structure Of Hppdmentioning

confidence: 99%

Section: The Structure Of Hppdmentioning

confidence: 99%

See 2 more Smart Citations

4-Hydroxyphenylpyruvate Dioxygenase Inhibitors: From Chemical Biology to Agrochemicals

Ndikuryayo

Moosavi

Yang

et al. 2017

J. Agric. Food Chem.

106

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“…En effet,leur activité est inhibée lorsqu'il est rem-dine hydroxylase; la lysine hydroxylase, la triméthylelysi->ur 1< phalosporine hydroxylase et la hydroxyphénylpyruvate dioxy-+ 2 + 2 place par du Zn ou du Pd . Cette demande en ion ferreux est (2) prouvée aussi bien pour la butyrobetame hydroxylase, la proline 4-hydroxylase, la proline 3-hydroxylase, ' la thymidine hydroxylase; la lysine hydroxylase, la triméthylel^ ne hydroxylase; que pour la thymine oxygenase; ' ' la iporine 1 (33)(34)(35) genäse. f) Elles demandent la présence non stoechiométrique d'un agent réducteur qui est l'acide ascorbique.…”

Section: Définition Et Classification Des Oxygenasesunclassified

Decarboxylation Oxydative Des Acides Α-Cetoniques. Modeles Pour l'HYDROXYLATIONBIOLOGIQUE

Αγορίτσα-Εξάρχου¹

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Chemistry and biology of vitamin E

Schneider¹

2004

Mol. Nutr. Food Res.

467

271

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Our understanding of the role of vitamin E in human nutrition, health, and disease has broadened and changed over the past two decades. Viewed initially as nature's most potent lipid-soluble antioxidant (and discovered for its crucial role in mammalian reproduction) we have now come to realize that vitamin E action has many more facets, depending on the physiological context. Although mainly acting as an antioxidant, vitamin E can also be a pro-oxidant; it can even have nonantioxidant functions: as a signaling molecule, as a regulator of gene expression, and, possibly, in the prevention of cancer and atherosclerosis. Since the term vitamin E encompasses a group of eight structurally related tocopherols and tocotrienols, individual isomers have different propensities with respect to these novel, nontraditional roles. The particular beneficial effects of the individual isomers have to be considered when dissecting the physiological impact of dietary vitamin E or supplements (mainly containing only the alpha-tocopherol isomer) in clinical trials. These considerations are also relevant for the design of transgenic crop plants with the goal of enhancing vitamin E content because an engineered biosynthetic pathway may be biased toward formation of one isomer. In contrast to the tremendous recent advances in knowledge of vitamin E chemistry and biology, there is little hard evidence from clinical and epidemiologic studies on the beneficial effects of supplementation with vitamin E beyond the essential requirement.

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Purification and properties of avian liver p-hydroxyphenylpyruvate hydroxylase.

Cited by 47 publications

References 27 publications

4-Hydroxyphenylpyruvate Dioxygenase Inhibitors: From Chemical Biology to Agrochemicals

4-Hydroxyphenylpyruvate Dioxygenase Inhibitors: From Chemical Biology to Agrochemicals

Decarboxylation Oxydative Des Acides Α-Cetoniques. Modeles Pour l'HYDROXYLATIONBIOLOGIQUE

Chemistry and biology of vitamin E

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