Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Amycolatopsis orientalis |
Protein Variants | Comment | Organism |
---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | a Fe(II)-dependent dioxygenase | Amycolatopsis orientalis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxyphenylpyruvate + O2 | Amycolatopsis orientalis | - |
4-hydroxymandelate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Amycolatopsis orientalis | - |
gene AOHMS | - |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes by ammonium sulfate fractionation, anion echange chromatography, and gel filtration | Amycolatopsis orientalis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2 | reaction mechanism, overview | Amycolatopsis orientalis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxyphenylpyruvate + O2 | - |
Amycolatopsis orientalis | 4-hydroxymandelate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HMS | - |
Amycolatopsis orientalis |
hydroxymandelate synthase | - |
Amycolatopsis orientalis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Amycolatopsis orientalis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Amycolatopsis orientalis |
General Information | Comment | Organism |
---|---|---|
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 |