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Literature summary for 1.13.11.27 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
Search for more literature for 1.13.11.27

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes Streptomyces avermitilis

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylpyruvate + O2 Streptomyces avermitilis
-
 homogentisate + CO2 + 4-hydroxyphenylacetate the wild-type enzyme produces 90% homogentisate, 1% quinolacetate, and 9% 4-hydroxyphenylacetate ?

Organism

Organism UniProt Comment Textmining
Streptomyces avermitilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Streptomyces avermitilis

Reaction

Reaction Comment Organism Reaction ID
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 reaction mechanism, overview Streptomyces avermitilis
a

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
HPPD
-
 Streptomyces avermitilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Streptomyces avermitilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Streptomyces avermitilis

General Information

General Information Comment Organism
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