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 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/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/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/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 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 Y116F no changes in the C1:C4 oxidation ratio -, 745380 1.14.99.53 Y142A distance between the copper ion and the predicted active site residue are increased -, 766407 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 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