Cloned (Comment) | Organism |
---|---|
expression of C-terminally strep-tagged enzyme in Escherichia coli strain BL21(DE3) | Streptomyces coelicolor |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetic analysis, overview | Streptomyces coelicolor | |
0.035 | - |
2-oxo-4-phenylbutanoic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
0.16 | - |
4-methoxyphenylpyruvic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
0.22 | - |
4-hydroxyphenylpyruvate | pH 7.5, 25°C | Streptomyces coelicolor | |
0.353 | - |
phenylpyruvic acid | pH 7.5, 25°C | Streptomyces coelicolor |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | a nonheme Fe(II) dependent dioxygenase | Streptomyces coelicolor |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxyphenylpyruvate + O2 | Streptomyces coelicolor | - |
4-hydroxymandelate + CO2 | - |
? | |
4-hydroxyphenylpyruvate + O2 | Streptomyces coelicolor A3(2) | - |
4-hydroxymandelate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces coelicolor | - |
- |
- |
Streptomyces coelicolor A3(2) | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally strep-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography | Streptomyces coelicolor |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxo-4-phenylbutanoic acid + O2 | - |
Streptomyces coelicolor | ? | - |
? | |
2-oxo-4-phenylbutanoic acid + O2 | - |
Streptomyces coelicolor A3(2) | ? | - |
? | |
4-fluorophenylpyruvic acid + O2 | - |
Streptomyces coelicolor | ? | - |
? | |
4-fluorophenylpyruvic acid + O2 | - |
Streptomyces coelicolor A3(2) | ? | - |
? | |
4-hydroxyphenylpyruvate + O2 | - |
Streptomyces coelicolor | 4-hydroxymandelate + CO2 | - |
? | |
4-hydroxyphenylpyruvate + O2 | - |
Streptomyces coelicolor A3(2) | 4-hydroxymandelate + CO2 | - |
? | |
4-methoxyphenylpyruvic acid + O2 | - |
Streptomyces coelicolor | ? | - |
? | |
4-methoxyphenylpyruvic acid + O2 | - |
Streptomyces coelicolor A3(2) | ? | - |
? | |
4-methylphenylpyruvic acid + O2 | - |
Streptomyces coelicolor | ? | - |
? | |
4-nitrophenylpyruvic acid + O2 | - |
Streptomyces coelicolor | ? | - |
? | |
additional information | substrate specificity, overview, Hms accepts a range of 2-oxo acids, whereby the presence of an aromatic substituent is crucial for efficient substrate turnover. A hydrophobic substrate binding pocket is identified as the likely determinant of substrate specificity. The enzyme shows high regioselectivity of oxygenation and a strong coupling efficiency of C-C bond cleavage and subsequent hydroxylation. The turnover number of Hms strongly correlates with substrate hydrophobicity. Quantitative structure activity relationship and in silico docking analyses, e.g. with (S)-mandelate and (R)-mandelate, overview | Streptomyces coelicolor | ? | - |
? | |
additional information | substrate specificity, overview, Hms accepts a range of 2-oxo acids, whereby the presence of an aromatic substituent is crucial for efficient substrate turnover. A hydrophobic substrate binding pocket is identified as the likely determinant of substrate specificity. The enzyme shows high regioselectivity of oxygenation and a strong coupling efficiency of C-C bond cleavage and subsequent hydroxylation. The turnover number of Hms strongly correlates with substrate hydrophobicity. Quantitative structure activity relationship and in silico docking analyses, e.g. with (S)-mandelate and (R)-mandelate, overview | Streptomyces coelicolor A3(2) | ? | - |
? | |
phenylpyruvic acid + O2 | - |
Streptomyces coelicolor | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
(S)-hydroxymandelate synthase | - |
Streptomyces coelicolor |
4-(S) hydroxymandelate synthase | - |
Streptomyces coelicolor |
HMS | - |
Streptomyces coelicolor |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Streptomyces coelicolor |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.035 | - |
4-nitrophenylpyruvic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
0.077 | - |
4-fluorophenylpyruvic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
0.13 | - |
4-methylphenylpyruvic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
0.17 | - |
2-oxo-4-phenylbutanoic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
0.88 | - |
phenylpyruvic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
0.96 | - |
4-methoxyphenylpyruvic acid | pH 7.5, 25°C | Streptomyces coelicolor | |
4.5 | - |
4-hydroxyphenylpyruvate | pH 7.5, 25°C | Streptomyces coelicolor |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Streptomyces coelicolor |
General Information | Comment | Organism |
---|---|---|
malfunction | upon introduction of a steric barrier, which is suspected to obstruct the accommodation of the aromatic ring in the hydrophobic pocket during the final hydroxylation step, the racemization of product is obtained | Streptomyces coelicolor |