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	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	Y142A	distance between the copper ion and the predicted active site residue are increased	-, 766407	
1.14.99.53	Y116F	no changes in the C1:C4 oxidation ratio	-, 745380	
1.14.99.53	W88Y/N91F	mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54	-, 745380	
1.14.99.53	W82Y/N85F/Y116F/Q141W	loss of chitin oxidizinbg activity, 10.2% residual cellulose C1- and 1.6% residual C4-oxidizing activity, ratio C1:C4-activity is 5.78	745380	
1.14.99.53	W82Y/N85F/Y116F/Q141W	mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.8	745380	
1.14.99.53	W82Y/N85F/Y116F	mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 14.7	745380	
1.14.99.53	W82Y/N85F/Q141W	loss of chitin monooxygenase activity, 12.21% residual cellulose C1- and 2.1% residual C4-oxidizing activity, ratio C1:C4-activity is 5.06	745380	
1.14.99.53	W82Y/N85F/Q141W	mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.1	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	
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	N85F	mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9	-, 745380	
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	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	H61A	distance between the copper ion and the predicted active site residue are increased	-, 766407	
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	D140A	mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity	-, 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	A148G	mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54	-, 745380