EC Number   |
Protein Variants |
Reference |
|---|
   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 | H1A |
hydrogen bonds between the copper ion and the predicted active site residues are similar to wild-type |
-, 766407 |
| 1.14.99.53 | H61A |
distance between the copper ion and the predicted active site residue are increased |
-, 766407 |
| 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 | 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 | N80D/F82A/Y111F/W141Q |
mutations of the substrate-binding surface, decreases thermal stability. Mutant is exclusively C1-oxidizing and displays activity on chitin and cellulose |
767106 |
| 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 |
