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EC Number
Amino acid exchange
Commentary
Reference
A143C/P183C/S73C/A115C
introduction of addtitional disulfide bridges A143C-P183C and S73C-A115C, increase in melting temperature by 12 degrees
A143C/P183C/S73C/A115C
introduction of addtitional disulfide bridges A143C-P183C and S73C-A115C, increase in melting temperature by 12 degrees; 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
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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
A148G
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
A148S
mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54
D140A
mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity
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
more
introduction of additional disulfide bridges. Four out of 16 variants display an improvement in melting temperature, ranging from 2°C to 9°C
more
introduction of additional disulfide bridges. Four out of 16 variants display an improvement in melting temperature, ranging from 2°C to 9°C; 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
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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
Results 1 - 10 of 20 > >>