Alkaptonuria and Cervical Disc Herniation: Case Report. [PDF]
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Specific knockout of kidney homogentisate 1,2-dioxygenase reveals that local metabolism of tyrosine and homogentisic acid is negligible in alkaptonuria. [PDF]
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High-yield production of hydroxytyrosol through metabolic engineering of <i>Yarrowia lipolytica</i>. [PDF]
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Therapeutic adenine base editor with minimized off-target effects. [PDF]
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Cardiovascular involvement in Alcaptonuria: a case report on ochronotic aortic valve. [PDF]
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Shikimate crosstalk enables record-level homogentisic acid production in <i>Yarrowia lipolytica</i>. [PDF]
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4-Hydroxyphenylpyruvate dioxygenase
Archives of Biochemistry and Biophysics, 20054-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.
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On 4-hydroxyphenylpyruvate dioxygenase of adult frog liver
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19821. 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.
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Novel Pyrazole Amides as Potential 4-Hydroxyphenylpyruvate Dioxygenase Inhibitors
Journal of Agricultural and Food Chemistry, 20224-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 ...
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Human 4‐hydroxyphenylpyruvate dioxygenase
European Journal of Biochemistry, 1993We 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.
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