EC Number   |
Protein Variants |
Reference  |
|---|
   1.14.99.53 | Y56W |
mutation shows no detectable effect on substrate-binding preferences but, in synergy experiments with chitinases, the mutant appears to be more efficient on alpha-chitin |
-, 740434 |
| 1.14.99.53 | more |
removal of the chitin-binding modules reduces LPMO activity toward alpha-chitin. The full-length enzyme and the individual catalytic LPMO module boost the activity of an endochitinase equally well |
740758 |
| 1.14.99.53 | Y54A |
mutation of residue at subsite -4, minimal effect on degradation of beta-chitin, about 20% residual activity with substrate [(1->4)-N-acetyl-beta-D-glucosaminyl]6 |
744375 |
| 1.14.99.53 | A148G |
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54 |
-, 745380 |
| 1.14.99.53 | A148S |
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54 |
-, 745380 |
| 1.14.99.53 | D140A |
mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity |
-, 745380 |
| 1.14.99.53 | more |
neither truncation of theLPMO10B family 2 carbohydrate-binding module nor mutations altering access to the solvent-exposed axial copper coordination site significantly change the C1:C4 oxidation ratio |
-, 745380 |
| 1.14.99.53 | N85F |
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9 |
-, 745380 |
| 1.14.99.53 | W82Y |
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 2.0 |
-, 745380 |
| 1.14.99.53 | W82Y/N85F |
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 10.9 |
745380 |
