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