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Literature summary extracted from

  • Raspail, C.; Graindorge, M.; Moreau, Y.; Crouzy, S.; Lefebvre, B.; Robin, A.Y.; Dumas, R.; Matringe, M.
    4-hydroxyphenylpyruvate dioxygenase catalysis: identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme (2011), J. Biol. Chem., 286, 26061-26070.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.27 N261D site-directed mutagenesis, during the reaction mechanism, the last 1,2 rearrangement is blocked in S246A HPPD mutant, so that an arene oxide-derived intermediate is released as an alternative product, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
1.13.11.27 N275D site-directed mutagenesis Daucus carota
1.13.11.27 P214T site-directed mutagenesis, during hte reaction mechanism, the last 1,2 rearrangement is blocked in S246A HPPD mutant, so that an arene oxide-derived intermediate is released as an alternative product Pseudomonas fluorescens
1.13.11.27 Q272E site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
1.13.11.27 Q286E site-directed mutagenesis Daucus carota
1.13.11.27 Q286E site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
1.13.11.27 Q300E site-directed mutagenesis Daucus carota
1.13.11.27 Q358E site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
1.13.11.27 Q372E site-directed mutagenesis Daucus carota
1.13.11.27 S246A site-directed mutagenesis, during the reaction mechanism, the last 1,2 rearrangement is blocked in S246A HPPD mutant, so that an arene oxide-derived intermediate is released as an alternative product, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
1.13.11.27 S260A site-directed mutagenesis Daucus carota

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.27 0.0075
-
 4-hydroxyphenylpyruvate recombinant wild-type enzyme, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.009
-
 4-hydroxyphenylpyruvate recombinant mutant S246A, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.153
-
 4-hydroxyphenylpyruvate recombinant mutant N261D, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.286
-
 4-hydroxyphenylpyruvate recombinant mutant Q358E, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.452
-
 4-hydroxyphenylpyruvate recombinant mutant Q272E, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.551
-
 4-hydroxyphenylpyruvate recombinant mutant Q286E, pH and temperature not specified in the publication Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.27 4-hydroxyphenylpyruvate + O2 Arabidopsis thaliana
-
 homogentisate + CO2
-
 ?
1.13.11.27 4-hydroxyphenylpyruvate + O2 Pseudomonas fluorescens
-
 homogentisate + CO2
-
 ?
1.13.11.27 4-hydroxyphenylpyruvate + O2 Daucus carota
-
 homogentisate + CO2
-
 ?
1.13.11.27 4-hydroxyphenylpyruvate + O2 Streptomyces avermitilis
-
 homogentisate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.27 Arabidopsis thaliana
-
-
-
1.13.11.27 Daucus carota
-
-
-
1.13.11.27 Pseudomonas fluorescens
-
-
-
1.13.11.27 Streptomyces avermitilis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 direct involvement of the arene oxide intermediate to the reaction mechanism Arabidopsis thaliana
a
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 direct involvement of the arene oxide intermediate to the reaction mechanism Pseudomonas fluorescens
a
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 direct involvement of the arene oxide intermediate to the reaction mechanism Daucus carota
a
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 direct involvement of the arene oxide intermediate to the reaction mechanism Streptomyces avermitilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.27 4-hydroxyphenylpyruvate + O2
-
 Arabidopsis thaliana homogentisate + CO2
-
 ?
1.13.11.27 4-hydroxyphenylpyruvate + O2
-
 Pseudomonas fluorescens homogentisate + CO2
-
 ?
1.13.11.27 4-hydroxyphenylpyruvate + O2
-
 Daucus carota homogentisate + CO2
-
 ?
1.13.11.27 4-hydroxyphenylpyruvate + O2
-
 Streptomyces avermitilis homogentisate + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.27 HPPD
-
 Arabidopsis thaliana
1.13.11.27 HPPD
-
 Pseudomonas fluorescens
1.13.11.27 HPPD
-
 Daucus carota
1.13.11.27 HPPD
-
 Streptomyces avermitilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.27 30
-
 assay at Arabidopsis thaliana
1.13.11.27 30
-
 assay at Pseudomonas fluorescens
1.13.11.27 30
-
 assay at Daucus carota
1.13.11.27 30
-
 assay at Streptomyces avermitilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.27 0.1
-
 4-hydroxyphenylpyruvate recombinant mutant Q286E, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.2
-
 4-hydroxyphenylpyruvate recombinant mutant Q272E, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.2
-
 4-hydroxyphenylpyruvate recombinant mutant S246A, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 0.3
-
 4-hydroxyphenylpyruvate recombinant mutant N261D, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 1.8
-
 4-hydroxyphenylpyruvate recombinant wild-type enzyme, pH and temperature not specified in the publication Arabidopsis thaliana
1.13.11.27 2.1
-
 4-hydroxyphenylpyruvate recombinant mutant Q358E, pH and temperature not specified in the publication Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.13.11.27 additional information 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 Pseudomonas fluorescens
1.13.11.27 additional information 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 Streptomyces avermitilis
1.13.11.27 additional information 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 Daucus carota
1.13.11.27 additional information 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 Arabidopsis thaliana