Results 151 to 160 of about 12,760,006 (203)

4-Hydroxyphenylpyruvate dioxygenase

Archives of Biochemistry and Biophysics, 2005
4-Hydroxyphenylpyruvate dioxygenase (HPPD) is an Fe(II)-dependent, non-heme oxygenase that catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisate. This reaction involves decarboxylation, substituent migration and aromatic oxygenation in a single catalytic cycle.
Graham Moran
exaly   +3 more sources

4-Hydroxyphenylpyruvate Dioxygenase Inhibitors: From Chemical Biology to Agrochemicals

Journal of Agricultural and Food Chemistry, 2017
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 ...
Ferdinand Ndikuryayo   +2 more
exaly   +3 more sources

The hydroxyphenylpyruvate dioxygenase fromSynechocystissp. PCC 6803 is not required for plastoquinone biosynthesis [PDF]

open access: yesFEBS Letters, 2002
The disruption of the Synechocystis open reading frame Δslr0090 encoding a gene with high homology to plant genes encoding 4-hydroxyphenylpyruvate dioxygenase results in an impairment of tocopherol biosynthesis without affecting levels of plastoquinone ...
Jens Appel, Karin Krupińska
exaly   +2 more sources

Discovery of Novel Pyrazole Derivatives with Improved Crop Safety as 4-Hydroxyphenylpyruvate Dioxygenase-Targeted Herbicides

open access: yesJournal of Agricultural and Food Chemistry, 2023
As one of the essential herbicide targets, 4-hydroxyphenylpyruvate dioxygenase (HPPD) has recently been typically used to produce potent new herbicides.
Xiuhai Gan
exaly   +2 more sources

4-Hydroxyphenylpyruvate dioxygenase as a drug discovery target

Drug News & Perspectives, 2003
The molecular mechanism for 4-hydroxyphenylpyruvate dioxygenase (4-HPPD) inhibition by nitisinone, a recently approved new drug for the treatment of hereditary tyrosinemia type I, has been satisfactorily explained by its action as an analogue to the substrate 4-hydroxyphenylpyruvate.
Chung-Shieh, Wu   +3 more
openaire   +4 more sources

On 4-hydroxyphenylpyruvate dioxygenase of adult frog liver

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1982
1. It has been reported that 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) activity in the liver from Rana esculenta is present only after autolysis of trypsin digestion, which releases a heat-and acid-stable inhibitor of low molecular mass. 2. Attempts to demonstrate similar effects with the liver enzyme from adult Rana pipiens were unsuccessful.
S, Lindstedt, B, Odelhög, M, Rundgren
openaire   +2 more sources

Novel Pyrazole Amides as Potential 4-Hydroxyphenylpyruvate Dioxygenase Inhibitors

Journal of Agricultural and Food Chemistry, 2022
4-Hydroxyphenylpyruvate dioxygenase (HPPD) is an important target for the development of new herbicides. HPPD inhibitors can hinder photosynthesis and induce weed death with bleaching symptoms. To explore the novel skeleton of HPPD inhibitors, a series of novel pyrazole amide derivatives were synthesized and evaluated for their inhibitory effects on ...
Huanan Zeng   +5 more
openaire   +2 more sources

Human 4‐hydroxyphenylpyruvate dioxygenase

European Journal of Biochemistry, 1993
We report the primary structure of 4‐hydroxyphenylpyruvate dioxygenase [4‐hydroxyphenylpyruvate: oxygen oxidoreductase (hydroxylating, decarboxylating)]. The work is based on the isolation of cDNA clones from human liver λgt11 libraries. Several overlapping clones covering the coding sequence were characterized.
U, Rüetschi   +5 more
openaire   +2 more sources

Alternate substrates and inhibitors of bacterial 4-hydroxyphenylpyruvate dioxygenase

Biochemistry, 1985
A variety of analogues of (4-hydroxyphenyl)pyruvic acid were synthesized, and the reactions of these compounds with the 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. P.J. 874 were examined. Several of the ring-substituted substrate analogues are reversible inhibitors of the enzyme, the most potent being the competitive inhibitor (2,6 ...
R A, Pascal, M A, Oliver, Y C, Chen
openaire   +2 more sources

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