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	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	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	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