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Literature summary for 1.13.11.27 extracted from

  • Moran, G.
    4-Hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase exemplars of the alpha-keto acid dependent oxygenases (2014), Arch. Biochem. Biophys., 544, 58-68 .
    View publication on PubMed

Application

Application Comment Organism
agriculture the enzyme is a target for herbicides, e.g. triketone inhibitors Arabidopsis thaliana
drug development the enzyme is a target for inhibitor and herbicide development Arabidopsis thaliana
drug development the human enzyme is a target for drug development in treatment of type 1 tyrosinemia, alkaptonuria, and hawkinsinuria, overvuew Homo sapiens

Protein Variants

Protein Variants Comment Organism
N245S site-directed mutagenesis, the mutant produces quinolacetic acid as reaction product Streptomyces avermitilis

Inhibitors

Inhibitors Comment Organism Structure
isoxaflutole
-
Arabidopsis thaliana
leptospermone
-
Arabidopsis thaliana
mesotrione
-
Arabidopsis thaliana
additional information inhibition mechanism of enzyme HPPD, detailed overview Arabidopsis thaliana
additional information inhibition mechanism of enzyme HPPD, detailed overview Homo sapiens
additional information inhibition mechanism of enzyme HPPD, detailed overview Paracoccidioides brasiliensis
additional information inhibition mechanism of enzyme HPPD, detailed overview Pseudomonas fluorescens
additional information inhibition mechanism of enzyme HPPD, detailed overview Streptomyces avermitilis
nitisinone i.e. orfadin or NTBC, an effective herbicide Arabidopsis thaliana
nitisinone i.e. orfadin or NTBC, addition of NTBC halts the morphology transition and stems pathogenesis in this organism Paracoccidioides brasiliensis
nitisinone i.e. orfadin or NTBC, bidentate coordination of NTBC with the HPPD active site ferrous ion, enzyme-bound crystal structure, overview Streptomyces avermitilis
sulcotrione
-
Arabidopsis thaliana
tembotrione
-
Arabidopsis thaliana
usnic acid
-
Arabidopsis thaliana

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ involved in catalysis Pseudomonas fluorescens
Fe2+ involved in catalysis Paracoccidioides brasiliensis
Fe2+ involved in catalysis Arabidopsis thaliana
Fe2+ involved in catalysis Streptomyces avermitilis
Fe2+ involved in catalysis Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylpyruvate + O2 Pseudomonas fluorescens
-
homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2 Paracoccidioides brasiliensis
-
homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2 Arabidopsis thaliana
-
homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2 Streptomyces avermitilis
-
homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2 Homo sapiens
-
homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2 Streptomyces avermitilis ATCC 31267
-
homogentisate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P93836
-
-
Homo sapiens P32754
-
-
Paracoccidioides brasiliensis
-
-
-
Pseudomonas fluorescens
-
-
-
Streptomyces avermitilis Q53586
-
-
Streptomyces avermitilis ATCC 31267 Q53586
-
-

Reaction

Reaction Comment Organism Reaction ID
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 dioxygen reactivity and the common decarboxylation half reaction, and the hydroxylation half reaction, mechanisms, detailed overview Paracoccidioides brasiliensis
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 dioxygen reactivity and the common decarboxylation half reaction, and the hydroxylation half reaction, mechanisms, detailed overview Arabidopsis thaliana
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 dioxygen reactivity and the common decarboxylation half reaction, and the hydroxylation half reaction, mechanisms, detailed overview Streptomyces avermitilis
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 dioxygen reactivity and the common decarboxylation half reaction, and the hydroxylation half reaction, mechanisms, detailed overview Homo sapiens
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 dioxygen reactivity and the common decarboxylation half reaction, and the hydroxylation half reaction, mechanisms, inhibitor-bound crystal structure, PDB ID 1CJX, analysis, detailed overview Pseudomonas fluorescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylpyruvate + O2
-
Pseudomonas fluorescens homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2
-
Paracoccidioides brasiliensis homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2
-
Arabidopsis thaliana homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2
-
Streptomyces avermitilis homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2
-
Homo sapiens homogentisate + CO2
-
?
4-hydroxyphenylpyruvate + O2
-
Streptomyces avermitilis ATCC 31267 homogentisate + CO2
-
?

Synonyms

Synonyms Comment Organism
HPD
-
Streptomyces avermitilis
HPPD
-
Pseudomonas fluorescens
HPPD
-
Paracoccidioides brasiliensis
HPPD
-
Arabidopsis thaliana
HPPD
-
Streptomyces avermitilis
HPPD
-
Homo sapiens

Expression

Organism Comment Expression
Paracoccidioides brasiliensis enzyme HPPD is upregulated during the hyphal to yeast morphological transition that occurs when Paracoccidiodes brasiliensis fungus becomes pathogeneic up

General Information

General Information Comment Organism
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 Pseudomonas fluorescens
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 Paracoccidioides brasiliensis
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 Arabidopsis thaliana
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 Streptomyces avermitilis
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 Homo sapiens
additional information enzyme structure analysis, overview Pseudomonas fluorescens
additional information enzyme structure analysis, overview Paracoccidioides brasiliensis
additional information enzyme structure analysis, overview Arabidopsis thaliana
additional information enzyme structure analysis, overview Streptomyces avermitilis
additional information enzyme structure analysis, overview Homo sapiens
physiological function enzyme HPPD is upregulated during the hyphal to yeast morphological transition that occurs when Paracoccidiodes brasiliensis fungus becomes pathogeneic Paracoccidioides brasiliensis
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 Arabidopsis thaliana