EC Number   |
Inhibitors  |
Structure |
|---|
    3.2.1.2 | 2,3-epoxypropyl-alpha-D-glucopyranoside |
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172, inactivation mechanism |
   |
| 3.2.1.2 | 2-mercaptoethanol |
4%, 1h, activity is decreased to 53% |
|
| 3.2.1.2 | 3,4-epoxybutyl-alpha-D-glucopyranoside |
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172 |
|
| 3.2.1.2 | 4-chloromercuribenzoate |
inactivation, the enzyme can be reactivated by L-cysteine |
|
| 3.2.1.2 | 5,5'-dithiobis-(2-nitrobenzoic acid) |
chemical modification of the exposed sulfhydryl groups in beta-amylase from unmalted seeds with 5,5'-dithiobis-(2-nitrobenzoic acid) results in loss of activity. In the beta-amylase from malted seed the 5,5'-dithiobis-(2-nitrobenzoic acid) chemical modification results in the increase in the KM from 2.81 to 4.14 mg/ml |
|
| 3.2.1.2 | 5,5'-dithiobis-2-nitrobenzoate |
weak |
|
| 3.2.1.2 | acetic acid |
75% inhibition at 10 mM, 16.3% inhibition at 1 mM |
|
| 3.2.1.2 | acetone |
40%, relative activity is decreased to 87% |
|
| 3.2.1.2 | Ag+ |
- |
|
| 3.2.1.2 | Ag+ |
0.001-0.1 mM AgNO3 |
|
