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evolution
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4-hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase, HMS, EC 1.13.11.46, catalyze similar reactions using the same substrates, 4-hydroxyphenylpyruvate and dioxygen. Initially, both enzymes reduce and activate dioxygen in order to decarboxylate 4-hydroxyphenylpyruvate, yielding 4-hydroxyphenylacetate, CO2, and an activated oxo intermediate Both enzymes then hydroxylate 4-hydroxyphenylacetate but do so in different positions
evolution
the enzyme belongs to the non-haem Fe(II)/2-oxoacid-dependent oxygenase superfamily, which couples the oxidative decarboxylation of a 2-oxoacid (most commonly a-ketoglutarate) to the oxidation of the prime substrate
evolution
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4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS, EC 1.13.11.46) are outliers within the 2-oxo acid dependent oxygenase (aKAO) family. HPPD and HMS catalyze the chemistry of the majority of enzymes within the aKAO family but are clearly mechanistically convergent, having a grossly different structural topology. Some of the unique characteristics of HPPD and HMS have elucidated select parts of the catalytic cycle that are obscured in other family members. Moreover, the inhibitory chemistry of HPPD is a phenomenon with ever-expanding relevance across all kingdoms of life
evolution
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4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS, EC 1.13.11.46) are outliers within the 2-oxo acid dependent oxygenase (aKAO) family. HPPD and HMS catalyze the chemistry of the majority of enzymes within the aKAO family but are clearly mechanistically convergent, having a grossly different structural topology. Some of the unique characteristics of HPPD and HMS have elucidated select parts of the catalytic cycle that are obscured in other family members. Moreover, the inhibitory chemistry of HPPD is a phenomenon with ever-expanding relevance across all kingdoms of life
evolution
4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS, EC 1.13.11.46) are outliers within the 2-oxo acid dependent oxygenase (aKAO) family. HPPD and HMS catalyze the chemistry of the majority of enzymes within the aKAO family but are clearly mechanistically convergent, having a grossly different structural topology. Some of the unique characteristics of HPPD and HMS have elucidated select parts of the catalytic cycle that are obscured in other family members. Moreover, the inhibitory chemistry of HPPD is a phenomenon with ever-expanding relevance across all kingdoms of life
evolution
4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS, EC 1.13.11.46) are outliers within the 2-oxo acid dependent oxygenase (aKAO) family. HPPD and HMS catalyze the chemistry of the majority of enzymes within the aKAO family but are clearly mechanistically convergent, having a grossly different structural topology. Some of the unique characteristics of HPPD and HMS have elucidated select parts of the catalytic cycle that are obscured in other family members. Moreover, the inhibitory chemistry of HPPD is a phenomenon with ever-expanding relevance across all kingdoms of life
evolution
4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS, EC 1.13.11.46) are outliers within the 2-oxo acid dependent oxygenase (aKAO) family. HPPD and HMS catalyze the chemistry of the majority of enzymes within the aKAO family but are clearly mechanistically convergent, having a grossly different structural topology. Some of the unique characteristics of HPPD and HMS have elucidated select parts of the catalytic cycle that are obscured in other family members. Moreover, the inhibitory chemistry of HPPD is a phenomenon with ever-expanding relevance across all kingdoms of life
evolution
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4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS, EC 1.13.11.46) are outliers within the 2-oxo acid dependent oxygenase (aKAO) family. HPPD and HMS catalyze the chemistry of the majority of enzymes within the aKAO family but are clearly mechanistically convergent, having a grossly different structural topology. Some of the unique characteristics of HPPD and HMS have elucidated select parts of the catalytic cycle that are obscured in other family members. Moreover, the inhibitory chemistry of HPPD is a phenomenon with ever-expanding relevance across all kingdoms of life
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malfunction
deficiency in active 4-HPPD in humans results in type III tyrosinemia, a rare autosomal recessive disorder
malfunction
inhibition of HPPD can effectively alleviate the symptoms of type I tyrosinemia
malfunction
mutant plants with null alleles of HPPD are reported to exhibit a lethal photobleaching phenotype. MsHPPD expression in three MsHPPD-overexpressing transgenic lines and wild-type, overview
malfunction
neutrophil preparations from a patient with tyrosinemia type III, with inherited deficiency of 4-hydroxyphenylpyruvate dioxygenase (HPPD), exhibit a far higher NO release than controls, when NO is estimated in terms of nitrite content in the suspending media. L-tyrosine increases nitrite release and accumulation in suspending media of U-937 cells, a human monoblast-like lymphoma cell line which displays many characteristics of macrophages, including the expression of inducible and endothelial nitric oxide synthases. The increase of nitrite release by patient's neutrophils might be related to the presence of high L-tyrosine concentrations in the blood samples rather than to HPPD deficiency of in these cells
malfunction
when HPPD is inhibited, the plant is severely damaged by sunlight, becoming bleached and eventually undergoing necrosis and death. HPPD inhibitors are termed bleaching herbicides
metabolism
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inhibition mechanism of 2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione
metabolism
enzyme 4-HPPD catalyzes the second step in the pathway of tyrosine catabolism, the conversion of 4-hydroxyphenyl-pyruvate to homogentisate
metabolism
second step of oxidative tyrosine catabolism
metabolism
4-ydroxyphenylpyruvate dioxygenase (HPPD) is an essential enzyme in tyrosine catabolism
metabolism
enzyme HPPD is the first committed enzyme involved in the biosynthesis of vitamin E. Vitamin E is not a single compound, but rather the collective name for a group of eight lipid-soluble antioxidants consisting of a polar chromanol head group and a hydrophobic prenyl tail, which are derived from the methylerythritol-4-phosphate (MEP) and shikimate pathways. Four of these compounds are termed tocopherols, and the other four are termed tocotrienols, and depending on the saturation level of the hydrophobic tail and also the number and position of the methyl groups on the chromanol ring, members of the vitamin E group are classified into alpha-, beta-, gamma- and delta-forms. In plants, the production of HGA is the first step in tocopherol synthesis, and homogentisic acid (HGA) is synthesized from p-hydroxyphenyl pyruvate (HPP) in a reaction catalyzed by enzyme HPPD
metabolism
hydroxyphenylpyruvate dioxygenase catalyzes the second step in the pathway of L-tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate
metabolism
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suggested hydroxylation mechanisms for HMS and HPPD and pathways leading to alternative products: oxepinone and quinolacetate
metabolism
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the enzyme is involved in the second step of the tyrosine degradation pathway, catalyzing the conversion of 4-hydroxyphenylpyruvate to homogentisate
metabolism
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the enzyme is ivolved in the tyrosine catabolic pathway, it catalyzes the synthesis of the central compound homogentisate and plays an important role, overview
metabolism
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suggested hydroxylation mechanisms for HMS and HPPD and pathways leading to alternative products: oxepinone and quinolacetate
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metabolism
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second step of oxidative tyrosine catabolism
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physiological function
Vitis vinifera x Vitis vinifera
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involved in aromatic amino acid metabolism
physiological function
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involved in aromatic amino acid metabolism
physiological function
4-hydroxyphenylpyruvate dioxygenase is involved in vitamin E biosynthesis and abscisic acid-mediated seed germination in Medicago sativa. MsHPPD functions not only in the vitamin E biosynthetic pathway, but also plays a critical role in seed germination via affecting abscisic acid biosynthesis and signaling, overview. HPPD is essential for plant viability
physiological function
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enzyme HPPD activity is one of the key factors influencing the production of tocopherols, overview
physiological function
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enzyme HPPD is upregulated during the hyphal to yeast morphological transition that occurs when Paracoccidiodes brasiliensis fungus becomes pathogeneic
physiological function
the enzyme catalyzes the synthesis of homogentisate, a precursor of plastoquinone, a diene-dione molecule, that serves as a lipid soluble electron carrier linking photosystems and shuttling electrons through the electron transport chain. Homogentiate is also the precursor to tocopherols (vitamin E) that serve as antioxidants and plant hormones. As such photosynthetic life is inseparably dependent on tyrosine catabolism and nature has developed a number of allelopathic molecules that target HPPD and thus homogenetisate production
physiological function
heterologous expression results in thermosensitive pigmentation in Escherichia coli. The thermolability of HppD is responsible for the temperature-dependent melanization of Aeromonas salmonicida subsp. salmonicida
physiological function
HPD promotes tyrosine catabolism leading to increased acetyl-CoA levels, the source of histone acetylation, and also stimulates histone deacetylase 10 translocation from the nucleus into the cytoplasm mediated by tumor suppressor liver kinase B1-AMP-activated protein kinase signaling
physiological function
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Hppd participates in the catabolism of tyrosine and promotes pyomelanin production in Escherichia coli BL21. Injcetion of Apostichopus japonicus with the Hppd shows significantly stimulatory effects on the expression of oxidative stress related genes catalase, glutathione S-transferase, glutathione peroxidase, heat shock protein 70. At 48 h, the expression level of cytochrome P450 is down-regulated compared with cells treated with BSA
physiological function
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L-tyrosine catabolism plays a key role in pigment production in the test bacteria. The isolate produces deep brown pigments belonging to the pyomelanin group
physiological function
L-tyrosine catabolism plays a key role in pigment production in the test bacteria. The isolate produces deep brown pigments belonging to the pyomelanin group
physiological function
L-tyrosine catabolism plays a key role in pigment production in the test bacteria. The isolate produces deep brown pigments belonging to the pyomelanin group
additional information
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substrate binding, structure modeling, structure comparisons, quantum mechanical/molecular mechanical calculations of the enzyme-substrate complex and key reaction intermediates, overview. Residues Ser201, Asn216, Gln225, Gln239, and Gln309 are important for catalysis
additional information
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substrate binding, structure modeling, structure comparisons, quantum mechanical/molecular mechanical calculations of the enzyme-substrate complex and key reaction intermediates, overview. Residues Ser201, Asn216, Gln226, Gln230, and Gln305 are important for catalysis
additional information
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substrate binding, structure modeling, structure comparisons, quantum mechanical/molecular mechanical calculations of the enzyme-substrate complex and key reaction intermediates, overview. Residues Ser260, Asn275, Gln286, Gln300, and Gln372 are important for catalysis
additional information
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substrate binding, structure modeling, structure comparisons, quantum mechanical/molecular mechanical calculations of the enzyme-substrate complex and key reaction intermediates, overview. Three different models of HPP binding within the Arabidopsis thaliana HPPD active site. Residues Ser246, Asn261, Gln272, Gln286, and Gln358 are important for catalysis
additional information
the disordered C-terminal tail of the enzyme, which is extended C-terminus compared to other 4-HPPD enzymes, plays an important role in catalysis with a critical role of residue Q375 in orientating the tail and ensuring the conformation of the terminal alpha-helix to maintain the integrity of the active site for catalysis. The active site of 4-HPPD is enclosed by a C-terminal alpha-helix which is assumed to function as a gate which controls access of substrate. Interactions provided by Q375 to hold the terminal helix and the tail in proper position are critical for isolating the active site from solvent during catalysis, enzyme structure modeling, overview
additional information
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the disordered C-terminal tail of the enzyme, which is extended C-terminus compared to other 4-HPPD enzymes, plays an important role in catalysis with a critical role of residue Q375 in orientating the tail and ensuring the conformation of the terminal alpha-helix to maintain the integrity of the active site for catalysis. The active site of 4-HPPD is enclosed by a C-terminal alpha-helix which is assumed to function as a gate which controls access of substrate. Interactions provided by Q375 to hold the terminal helix and the tail in proper position are critical for isolating the active site from solvent during catalysis, enzyme structure modeling, overview
additional information
enzyme molecular docking study using crystal structure PDB ID 1SQI
additional information
enzyme molecular docking study using crystal structure PDB ID 1TG5. Three amino acid residues compose the active site: Gln358, His205 and Phe398
additional information
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enzyme structure analysis, overview
additional information
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enzyme structure analysis, overview
additional information
enzyme structure analysis, overview
additional information
enzyme structure analysis, overview
additional information
enzyme structure analysis, overview
additional information
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molecular dynamics simulations are performed for the HPPD-Fe(IV)=O-hydroxyphenylacetate complex in order to obtain a reliable starting structure for quantum mechanics/molecular mechanics calculations of ring hydroxylation and coupled rearrangement reactions catalyzed by the enzyme HPPD, structure of HPPD-Fe(II)-acetate complex, structure homology modeling, overview
additional information
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molecular dynamics simulations are performed for the HPPD-Fe(IV)=O-hydroxyphenylacetate complex in order to obtain a reliable starting structure for quantum mechanics/molecular mechanics calculations of ring hydroxylation and coupled rearrangement reactions catalyzed by the enzyme HPPD, structure of HPPD-Fe(II)-acetate complex, structure homology modeling, overview
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additional information
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enzyme structure analysis, overview
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