Results 11 to 20 of about 2,253 (135)
A novel enzymatic assay for the identification of 4-hydroxyphenylpyruvate dioxygenase modulators. [PDF]
STAR Protoc, 2023 4-hydroxyphenylpyruvate dioxygenase (HPPD) is a key enzyme involved in the pathogenesis of tyrosinemia III and cancer. Herein, we describe a spectroscopy-based assay to detect HPPD dioxygenase activity in the presence or absence of small-molecule modulators.
Parkins A, Pantouris G.
europepmc +4 more sources
4-hydroxyphenylpyruvate dioxygenase catalysis: identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme. [PDF]
J Biol Chem, 2011 4-Hydroxyphenylpyruvate dioxygenase (HPPD) catalyzes the conversion of 4-hydroxyphenylpyruvate (HPP) into homogentisate. HPPD is the molecular target of very effective synthetic herbicides. HPPD inhibitors may also be useful in treating life-threatening tyrosinemia type I and are currently in trials for treatment of Parkinson disease.
Raspail C +7 more
europepmc +3 more sources
Characterization of 4‐hydroxyphenylpyruvate dioxygenase [PDF]
European Journal of Biochemistry, 1992 The primary structure of Pseudomonas 4‐hydroxyphenylpyruvate dioxygenase was determined. Sequence degradation of the intact protein and of peptides from three different digests of the carboxymethylated protein established a 357‐residue polypeptide chain with a free α‐amino group.
U, Rüetschi +5 more
openaire +3 more sources
Human 4-Hydroxyphenylpyruvate Dioxygenase Gene (HPD)
Genomics, 1997 Overlapping DNA fragments spanning approximately 21 kb of genomic DNA and encompassing the human 4-hydroxyphenylpyruvate dioxygenase gene (HPD) have been cloned by screening a human leukocyte genomic library and by PCR amplification of human fibroblastic DNA.
U, Rüetschi, L, Rymo, S, Lindstedt
openaire +2 more sources
Inhibition of Barnyardgrass 4-Hydroxyphenylpyruvate Dioxygenase by Sulcotrione [PDF]
Plant Physiology, 1994 4-Hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) was partially purified from barnyardgrass (Echinochloa crus-galli L.) leaves and assayed by high-performance liquid chromatography analysis of product formation or by the capture of released 14CO2. The bleaching herbicide sulcotrione [2-(2-chloro-4-methanesulfonylbenzoyl)-1,3-cyclohexanedione] was ...
openaire +2 more sources
Evaluation of models for the mechanism of action of 4-hydroxyphenylpyruvate dioxygenase
Experientia, 1981 3-Hydroxyphenylpyruvic acid was oxygenated with various complexes of oxygen with Fe2+, superoxide ion, hydroperoxide anion, triplet and singlet oxygen. Oxidation occurred giving varying amounts of the 4-hydroxy derivatives of benzaldehyde, benzoic acid, phenol, phenylacetic acid and 4-carboxymethylquinone, but no homogentisic acid.
Jefford, Charles, Cadby, Peter Alan
openaire +3 more sources
The interaction of hydroxymandelate synthase with the 4-hydroxyphenylpyruvate dioxygenase inhibitor: NTBC [PDF]
Inorganica Chimica Acta, 2008 Hydroxymandelate synthase (HMS) catalyzes the committed step in the formation of para-hydroxyphenylglycine, a recurrent substructure of polycyclic non-ribosomal peptide antibiotics such as vancomycin. HMS uses the same substrates as 4-hydroxyphenylpyruvate dioxygenase (HPPD), 4-hydroxyphenylpyruvate (HPP) and O(2), and also conducts a dioxygenation ...
John A, Conrad, Graham R, Moran
openaire +2 more sources
The Crystal Structures of Zea mays and Arabidopsis 4-Hydroxyphenylpyruvate Dioxygenase [PDF]
Plant Physiology, 2004 Abstract The transformation of 4-hydroxyphenylpyruvate to homogentisate, catalyzed by 4-hydroxyphenylpyruvate dioxygenase (HPPD), plays an important role in degrading aromatic amino acids. As the reaction product homogentisate serves as aromatic precursor for prenylquinone synthesis in plants, the enzyme is an interesting target for ...
Fritze, I. +5 more
openaire +3 more sources
The C‐terminal of rat 4‐hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity [PDF]
FEBS Letters, 1996 We have cloned and overexpressed rat 4‐hydroxyphenylpyruvate dioxygenase (4HPPD) in Escherichia coli. The soluble, active recombinant enzyme was shown to contain both 4HPPD and α‐ketoisocaproate dioxygenase (αKICD) activity. However, upon truncation of the 14 amino acids at the C‐terminus by site‐directed mutagenesis, the resulting mutant enzyme (rat F
Lee, M +4 more
openaire +3 more sources
4-Hydroxyphenylpyruvate dioxygenase is an iron-tyrosinate protein.
Journal of Biological Chemistry, 1986 A resonance Raman investigation into the blue chromophore of 4-hydroxyphenylpyruvate dioxygenase, a non-heme iron enzyme from Pseudomonas P. J. 874, reveals the presence of enhanced vibrations characteristic of tyrosinate coordination to the iron center. The excitation profiles for these features show that they are associated with the 595 nm absorption
F C, Bradley +5 more
openaire +2 more sources