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Literature summary extracted from

  • Shah, D.; Conrad, J.; Moran, G.
    Intermediate partitioning kinetic isotope effects for the NIH shift of 4-hydroxyphenylpyruvate dioxygenase and the hydroxylation reaction of hydroxymandelate synthase reveal mechanistic complexity (2013), Biochemistry, 52, 6097-6107.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.27 recombinant expression of wild-type and mutant enzymes Streptomyces avermitilis
1.13.11.46 recombinant expression of wild-type and mutant enzymes Amycolatopsis orientalis

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.27 F364I site-directed mutagenesis, the mutant enzyme produces 47% homogentisate, 15% 4-hydroxyphenylacetate, and 19% quinolacetate, which differs from the wild-type activity Streptomyces avermitilis
1.13.11.27 N245D site-directed mutagenesis, the mutant enzyme produces 52% homogentisate and 26.8% 4-hydroxyphenylacetate, and 21.2% quinolacetate, which differs from the wild-type activity Streptomyces avermitilis
1.13.11.27 N245Q site-directed mutagenesis, the mutant enzyme produces 52% homogentisate and 45% 4-hydroxyphenylacetate, and 3% quinolacetate, which differs from the wild-type activity Streptomyces avermitilis
1.13.11.27 N245S site-directed mutagenesis, the mutant enzyme produces 3.4% homogentisate and 6.6% 4-hydroxyphenylacetate, and 90% quinolacetate, which differs from the wild-type activity Streptomyces avermitilis
1.13.11.27 P243T site-directed mutagenesis, the mutant enzyme produces 8.4% homogentisate, 46.5% 4-hydroxyphenylacetate, and 45% quinolacetate, which differs from the wild-type activity Streptomyces avermitilis
1.13.11.27 S230A site-directed mutagenesis, the mutant enzyme produces 7% homogentisate, 57% 4-hydroxyphenylacetate, and 36% quinolacetate, which differs from the wild-type activity Streptomyces avermitilis
1.13.11.46 S201A site-directed mutagenesis, the mutant enzyme produces 3% 4-hydroxyphenylacetate, and 97% 4-hydroxymandelate, the benzylic carbon retains predominant sp3 character in the TS for the initial hydrogen abstraction Amycolatopsis orientalis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.27 Fe2+ a Fe(II)-dependent dioxygenase, Fe2+ is involved in the catalytic mechanism binding to the substrate, overview Streptomyces avermitilis
1.13.11.46 Fe2+ a Fe(II)-dependent dioxygenase Amycolatopsis orientalis

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 Streptomyces avermitilis
-
homogentisate + CO2 + 4-hydroxyphenylacetate the wild-type enzyme produces 90% homogentisate, 1% quinolacetate, and 9% 4-hydroxyphenylacetate ?
1.13.11.46 4-hydroxyphenylpyruvate + O2 Amycolatopsis orientalis
-
4-hydroxymandelate + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.27 Streptomyces avermitilis
-
-
-
1.13.11.46 Amycolatopsis orientalis
-
gene AOHMS
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.27 recombinant wild-type and mutant enzymes by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Streptomyces avermitilis
1.13.11.46 recombinant wild-type and mutant enzymes by ammonium sulfate fractionation, anion echange chromatography, and gel filtration Amycolatopsis orientalis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 reaction mechanism, overview Streptomyces avermitilis
1.13.11.46 4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2 reaction mechanism, overview Amycolatopsis orientalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.27 4-hydroxyphenylpyruvate + O2
-
Streptomyces avermitilis homogentisate + CO2 + 4-hydroxyphenylacetate the wild-type enzyme produces 90% homogentisate, 1% quinolacetate, and 9% 4-hydroxyphenylacetate ?
1.13.11.46 4-hydroxyphenylpyruvate + O2
-
Amycolatopsis orientalis 4-hydroxymandelate + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.27 HPPD
-
Streptomyces avermitilis
1.13.11.46 HMS
-
Amycolatopsis orientalis
1.13.11.46 hydroxymandelate synthase
-
Amycolatopsis orientalis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.27 25
-
assay at Streptomyces avermitilis
1.13.11.46 25
-
assay at Amycolatopsis orientalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.27 7
-
assay at Streptomyces avermitilis
1.13.11.46 7
-
assay at Amycolatopsis orientalis

General Information

EC Number General Information Comment Organism
1.13.11.27 evolution 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 Streptomyces avermitilis
1.13.11.46 evolution 4-hydroxyphenylpyruvate dioxygenase, HPPD, EC 1.13.11.27, and hydroxymandelate synthase 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 Amycolatopsis orientalis