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 | Comment | Organism |
---|---|---|
N245S | site-directed mutagenesis, the mutant produces quinolacetic acid as reaction product | Streptomyces avermitilis |
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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | P93836 | - |
- |
Homo sapiens | P32754 | - |
- |
Paracoccidioides brasiliensis | - |
- |
- |
Pseudomonas fluorescens | - |
- |
- |
Streptomyces avermitilis | Q53586 | - |
- |
Streptomyces avermitilis ATCC 31267 | Q53586 | - |
- |
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 | 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 | Comment | Organism |
---|---|---|
HPD | - |
Streptomyces avermitilis |
HPPD | - |
Pseudomonas fluorescens |
HPPD | - |
Paracoccidioides brasiliensis |
HPPD | - |
Arabidopsis thaliana |
HPPD | - |
Streptomyces avermitilis |
HPPD | - |
Homo sapiens |
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 | 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 |