Crystallization (Comment) | Organism |
---|---|
- |
Priestia megaterium |
Protein Variants | Comment | Organism |
---|---|---|
V218F | the monophenolase activity of the mutant on L-tyrosine improves, as the Vmax and kcat values increase 4.2fold. Th same values for diphenolase activity on L-Dopa, however, decrease 2.1fold | Priestia megaterium |
V218G | in this mutant, the Vmax and kcat values towards L-tyrosine increase by 7.8fold and towards L-DOPA by 1.7fold, respectively | Priestia megaterium |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.05 | - |
L-tyrosine | wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
0.5 | - |
L-tyrosine | mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
0.8 | - |
L-Dopa | wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
1 | - |
L-Dopa | mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
1.1 | - |
L-Dopa | mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
1.4 | - |
L-tyrosine | mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-DOPA + O2 | Priestia megaterium | - |
L-dopachrome + H2O | - |
? | |
L-tyrosine + O2 | Priestia megaterium | - |
dopaquinone + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Priestia megaterium | B2ZB02 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-DOPA + O2 | - |
Priestia megaterium | L-dopachrome + H2O | - |
? | |
L-tyrosine + O2 | - |
Priestia megaterium | dopaquinone + H2O | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4 | - |
L-tyrosine | wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
16.7 | - |
L-tyrosine | mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
21 | - |
L-Dopa | wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
31.1 | - |
L-Dopa | mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
44.1 | - |
L-tyrosine | mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
73.3 | - |
L-Dopa | mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
11.9 | - |
L-tyrosine | mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
19.1 | - |
L-Dopa | wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
55.1 | - |
L-tyrosine | mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
62.1 | - |
L-Dopa | mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
73.7 | - |
L-Dopa | mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium | |
80 | - |
L-tyrosine | wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C | Priestia megaterium |