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Literature summary for 1.13.11.27 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
Search for more literature for 1.13.11.27

Protein Variants

Protein Variants Comment Organism
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
N275D site-directed mutagenesis Daucus carota
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
Q272E site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
Q286E site-directed mutagenesis Daucus carota
Q286E site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
Q300E site-directed mutagenesis Daucus carota
Q358E site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme Arabidopsis thaliana
Q372E site-directed mutagenesis Daucus carota
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
S260A site-directed mutagenesis Daucus carota

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

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

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

General Information

General Information Comment Organism
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
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
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
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