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	additional information	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	additional information	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