Crystallization (Comment) | Organism |
---|---|
crystals are obtained by hanging-drop vapour diffusion method. The enzyme is crystallized in the presence of the substrate D-2-chloropropionate at pH 5.5-6.4 and 4°C. 2.64 A resolution | Pseudomonas putida |
Protein Variants | Comment | Organism |
---|---|---|
D205E | activity with D-2-chloropropionate is 10.1% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 13fold higher compared to mutant enzyme | Pseudomonas putida |
D205N | no activity with D-2-chloropropionate | Pseudomonas putida |
F281A | activity with D-2-chloropropionate is 54.7% compared to activity of the wild-type enzyme | Pseudomonas putida |
G50A | activity with D-2-chloropropionate is 5.1% compared to activity of the wild-type enzyme | Pseudomonas putida |
I52G | activity with D-2-chloropropionate is 1.5% compared to activity of the wild-type enzyme | Pseudomonas putida |
L285I | activity with D-2-chloropropionate is 24.4% compared to activity of the wild-type enzyme | Pseudomonas putida |
L288I | activity with D-2-chloropropionate is 37.2% compared to activity of the wild-type enzyme | Pseudomonas putida |
M284C | activity with D-2-chloropropionate is 7.0% compared to activity of the wild-type enzyme | Pseudomonas putida |
N131D | activity with D-2-chloropropionate is 4.4% compared to activity of the wild-type enzyme | Pseudomonas putida |
N203A | activity with D-2-chloropropionate is 1.2% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 355fold higher compared to mutant enzyme | Pseudomonas putida |
N203S | activity with D-2-chloropropionate is 0.4% compared to activity of the wild-type enzyme | Pseudomonas putida |
S204A | activity with D-2-chloropropionate is 4.9% compared to activity of the wild-type enzyme | Pseudomonas putida |
S204T | activity with D-2-chloropropionate is 41.8% compared to activity of the wild-type enzyme | Pseudomonas putida |
V51F | activity with D-2-chloropropionate is 36.6% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 4fold higher compared to mutant enzyme | Pseudomonas putida |
W48A | activity with D-2-chloropropionate is 0.2% compared to activity of the wild-type enzyme | Pseudomonas putida |
Y134F | activity with D-2-chloropropionate is 0.1% compared to activity of the wild-type enzyme | Pseudomonas putida |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.94 | - |
D-2-chloropropionate | wild-type enzyme, pH 10.0, 30°C | Pseudomonas putida | |
2.9 | - |
D-2-chloropropionate | mutant enzyme V51F, pH 10.0, 30°C | Pseudomonas putida | |
4.13 | - |
D-2-chloropropionate | mutant enzyme D205E, pH 10.0, 30°C | Pseudomonas putida | |
12 | - |
D-2-chloropropionate | mutant enzyme N203A, pH 10.0, 30°C | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | Q52086 | - |
- |
Pseudomonas putida AJ1/23 | Q52086 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-2-chloropropionate + H2O | - |
Pseudomonas putida | L-2-hydroxypropionate + chloride | - |
? | |
D-2-chloropropionate + H2O | - |
Pseudomonas putida AJ1/23 | L-2-hydroxypropionate + chloride | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | - |
Pseudomonas putida |
Synonyms | Comment | Organism |
---|---|---|
D-2-haloacid dehalogenase | - |
Pseudomonas putida |
D-DEX | - |
Pseudomonas putida |
HadD AJ1 | - |
Pseudomonas putida |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.59 | - |
D-2-chloropropionate | mutant enzyme N203A, pH 10.0, 30°C | Pseudomonas putida | |
12.6 | - |
D-2-chloropropionate | mutant enzyme V51F, pH 10.0, 30°C | Pseudomonas putida | |
16.35 | - |
D-2-chloropropionate | wild-type enzyme, pH 10.0, 30°C | Pseudomonas putida | |
55 | - |
D-2-chloropropionate | mutant enzyme D205E, pH 10.0, 30°C | Pseudomonas putida |