EC Number |
Inhibitors |
Structure |
---|
3.1.1.6 | Cu2+ |
acetyl esterase activity |
|
3.1.1.6 | Cu2+ |
2.2% residual activity at 2 mM |
|
3.1.1.6 | D-xylose |
at low concentrations of 1-5 mM, altered activity with 4-nitrophenyl acetate as substrate |
|
3.1.1.6 | diisopropyl fluorophosphate |
- |
|
3.1.1.6 | dimethylarsinic acid |
binding mechanism |
|
3.1.1.6 | EDTA |
metal-chelating reduces enzymatic activity by ca. 33% |
|
3.1.1.6 | EDTA |
strong inhibitor, 10 mM, 18% residual activity, EST1, p-nitrophenyl acetate as substrate |
|
3.1.1.6 | eserine |
competitive, complete inhibition at 25 mM |
|
3.1.1.6 | ethyl acetate |
85.29% residual activity at 0.5 mM |
|
3.1.1.6 | Fe2+ |
- |
|