Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Streptomyces avermitilis |
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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces avermitilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration | Streptomyces avermitilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 | reaction mechanism, overview | Streptomyces avermitilis |
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 | Comment | Organism |
---|---|---|
HPPD | - |
Streptomyces avermitilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Streptomyces avermitilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Streptomyces avermitilis |
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 |