Cloned (Comment) | Organism |
---|---|
- |
Pinus tabuliformis |
Protein Variants | Comment | Organism |
---|---|---|
E66A | activity with 1-chloro-2,4-dinitrobenzene is 18.4fold lower than wild-type activity, activity with ethacrynic acid is 1.25fold higher than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is 3fold lower than wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is higher than the refolding of the wild-type enzyme | Pinus tabuliformis |
I54A | activity with 1-chloro-2,4-dinitrobenzene is 2fold lower than wild-type activity, activity with ethacrynic acid is 3.5fold higher than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is 2.8fold higher than wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is lower than the refolding of the wild-type enzyme | Pinus tabuliformis |
K40A | activity with 1-chloro-2,4-dinitrobenzene is 18fold lower than wild-type activity, activity with ethacrynic acid is 1.2fold lower than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is nearly identical to wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is lower than the refolding of the wild-type enzyme | Pinus tabuliformis |
S67A | activity with 1-chloro-2,4-dinitrobenzene is fold 21.6fold lower than wild-type activity, activity with ethacrynic acid is 1.13fold lower than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is 3.9fold lower than wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is higher than the refolding of the wild-type enzyme | Pinus tabuliformis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.47 | - |
GSH | 25°C, wild-type enzyme | Pinus tabuliformis | |
0.48 | - |
GSH | 25°C, mutant enzyme S67A | Pinus tabuliformis | |
0.57 | - |
GSH | 25°C, mutant enzyme K40A | Pinus tabuliformis | |
0.76 | - |
1-chloro-2,4-dinitrobenzene | 25°C, wild-type enzyme | Pinus tabuliformis | |
0.89 | - |
GSH | 25°C, mutant enzyme E66A | Pinus tabuliformis | |
1.42 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme S67A | Pinus tabuliformis | |
1.89 | - |
GSH | 25°C, mutant enzyme I54A | Pinus tabuliformis | |
3.13 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme I54A | Pinus tabuliformis | |
4.23 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme E66A | Pinus tabuliformis | |
4.96 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme K40A | Pinus tabuliformis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Pinus tabuliformis | the enzyme plays an importent role in stress tolerance and detoxification in plants | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pinus tabuliformis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Pinus tabuliformis |
Renatured (Comment) | Organism |
---|---|
wild-type enzyme shows 25.42% of the initial activity after denaturation and refolding, mutant K40A 20.51%, mutant I54A 8.51%, mutant E66A 51.68% and mutant S67A 34.33% | Pinus tabuliformis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-chloro-2,4-dinitrobenzene + GSH | - |
Pinus tabuliformis | S-(2,4-dinitrophenyl)glutathione + HCl | - |
? | |
4-nitrophenyl acetate + GSH | at 0.2% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme | Pinus tabuliformis | ? | - |
? | |
7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH | at 23% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme | Pinus tabuliformis | ? | - |
? | |
ethacrynic acid + GSH | at 8% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme | Pinus tabuliformis | ? | - |
? | |
additional information | the enzyme plays an importent role in stress tolerance and detoxification in plants | Pinus tabuliformis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PtGSTU1 | - |
Pinus tabuliformis |
tau class glutathione transferase | - |
Pinus tabuliformis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
15 min, mutant enzymes E66A and S67A retain about 15% of its initial activity, K40A and I54A retain 62% of their initial activity, wild-type enzyme retains 95% of its initial activity | Pinus tabuliformis |
60 | - |
15 min, complete inactivation of the mutant enzymes K40A, I54A, E66A and S67A, wild-type enzyme retains 41% of its initial activity | Pinus tabuliformis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.32 | - |
GSH | 25°C, mutant enzyme E66A | Pinus tabuliformis | |
0.35 | - |
GSH | 25°C, mutant enzyme S67A | Pinus tabuliformis | |
0.5 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme S67A | Pinus tabuliformis | |
0.52 | - |
GSH | 25°C, mutant enzyme K40A | Pinus tabuliformis | |
1.08 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme E66A | Pinus tabuliformis | |
1.7 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme K40A | Pinus tabuliformis | |
3.4 | - |
GSH | 25°C, mutant enzyme I54A | Pinus tabuliformis | |
4.75 | - |
1-chloro-2,4-dinitrobenzene | 25°C, mutant enzyme I54A | Pinus tabuliformis | |
6.48 | - |
GSH | 25°C, wild-type enzyme | Pinus tabuliformis | |
6.74 | - |
1-chloro-2,4-dinitrobenzene | 25°C, wild-type enzyme | Pinus tabuliformis |