EC Number |
Protein Variants |
Reference |
---|
1.14.99.54 | A143C/P183C/S73C/A115C |
introduction of addtitional disulfide bridges A143C-P183C and S73C-A115C, increase in melting temperature by 12 degrees |
-, 746362 |
1.14.99.54 | A143C/P183C/S73C/A115C |
introduction of two additional disulfide bridges, mutant displays a 12°C increase in melting temperature and is able to retain 60% of its activity after heat treatment |
-, 741358 |
1.14.99.54 | A148G |
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54 |
-, 745380 |
1.14.99.54 | A148S |
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54 |
-, 745380 |
1.14.99.54 | D140A |
mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity |
-, 745380 |
1.14.99.54 | more |
construction of a C-terminally truncated variant containing 21 residues of the predicted linker domain. The truncated variant exhibits reduced binding to cellulose and about 50% of wild-type activity on cellulose |
-, 745374 |
1.14.99.54 | more |
introduction of additional disulfide bridges. Four out of 16 variants display an improvement in melting temperature, ranging from 2°C to 9°C |
-, 741358 |
1.14.99.54 | more |
isotopical labeling of the apo-form of the 21.4 kDa catalytic domain and the 10.7 kDa carbohydrate binding domain of LPMO10C and recombinant expression in Escherichia coli and assignment of the backbone of full-length LPMO10C |
-, 744472 |
1.14.99.54 | more |
neither truncation of the LPMO10B 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 |
1.14.99.54 | N85F |
mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9 |
-, 745380 |