EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.27 | 11 | - |
4-hydroxyphenylpyruvate | Solvent is H2O. Steady-state analyses of 4-hydroxyphenylpyruvate dioxygenase using proteo-HPP, 2,3,5,6-tetradeutero-HPP, and proteo-HPP in deuterium oxide are carried out in 1 ml assays on a Hasetech oxygen electrode. The assay mixture include ferrous sulfate (10 microM), DTT (1mM), HPPD (500 nM), and HPP (0-1 mM) in 20 mM HEPES, pH (pD) 7.0, under conditions of atmospheric oxygen (350 microM at 5°C) | Streptomyces avermitilis | |
1.13.11.27 | 22 | - |
4-hydroxyphenylpyruvate | Solvent is H2O. Steady-state analyses of 4-hydroxyphenylpyruvate dioxygenase using proteo-HPP, 2,3,5,6-tetradeutero-HPP, and proteo-HPP in deuterium oxide are carried out in 1 ml assays on a Hasetech oxygen electrode. The assay mixture include ferrous sulfate (10 microM), DTT (1mM), HPPD (500 nM), and HPP (0-1 mM) in 20 mM HEPES, pH (pD) 7.0, under conditions of atmospheric oxygen (350 microM at 5°C) | Streptomyces avermitilis | |
1.13.11.27 | 54 | - |
4-hydroxyphenylpyruvate | Solvent is D2O. Steady-state analyses of 4-hydroxyphenylpyruvate dioxygenase using proteo-HPP, 2,3,5,6-tetradeutero-HPP, and proteo-HPP in deuterium oxide are carried out in 1 ml assays on a Hasetech oxygen electrode. The assay mixture include ferrous sulfate (10 microM), DTT (1mM), HPPD (500 nM), and HPP (0-1 mM) in 20 mM HEPES, pH (pD) 7.0, under conditions of atmospheric oxygen (350 microM at 5°C) | Streptomyces avermitilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.27 | Streptomyces avermitilis | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.13.11.27 | at 5°C or below | Streptomyces avermitilis |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.13.11.27 | 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 | The data of the rapid acid quench followd by HPLC product analysis, indicate that the homogenisate product is formed during one turnover, as the amount of product is equivalent to the enzyme-substrate complex at 191 ms. | Streptomyces avermitilis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.13.11.27 | additional information | - |
with substrate 2,3,5,6-tetraproteo 4-hydroxyphenylpyruvate and the solvent H2O Vmax = 1.9/s, with substrate 2,3,5,6-tetradeutero 4-hydroxyphenylpyruvate and the solvent H2O Vmax = 1.8/s, with substrate 2,3,5,6-tetraproteo 4-hydroxyphenylpyruvate and the solvent D2O Vmax = 0.86/s | Streptomyces avermitilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.27 | 4-hydroxyphenylpyruvate + O2 | - |
Streptomyces avermitilis | homogentisate + CO2 | - |
? | |
1.13.11.27 | additional information | Single turnover kinetics are observed spectrophotometrically by mixing equal volumes of the anaerobic enzyme-substrate complex and solutions containing molecular oxygen in the presence of saturating HPP using a stopped-flow spectrophotometer. k1 = 7.4 x 100000 /M/s, k2 = 74 /s, k3 = 13.2 /s, k4 = 1.6 /s, indicating the accumulation of three catalytic intermediates. The kinetic data observed with substrate substituted with deutererons for aromatic protons are not significantly different from those observed with the proteo substrate. The final phase in catalysis (k4), decreases to 0.7 /s in the presence of deuterium oxide solvent, indicating the involvement of a solvent-derived proton in this step. | Streptomyces avermitilis | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.27 | HPPD | - |
Streptomyces avermitilis |