EC Number |
Activating Compound |
Reference |
---|
3.1.1.74 | 16-hydroxyhexadecanoic acid |
is strongly induced in vitro by cutin monomer 16-hydroxyhexadecanoic acid |
691941 |
3.1.1.74 | DMF |
activates 10% at 40% v/v |
729000 |
3.1.1.74 | DMF |
activates 6% at 40% v/v |
729000 |
3.1.1.74 | DMSO |
activates 14% at 40% v/v |
729000 |
3.1.1.74 | DMSO |
activates 9% at 40% v/v |
729000 |
3.1.1.74 | more |
absence of interfacial activation |
208329 |
3.1.1.74 | more |
no activation in the presence of Triton X-100 due to the absence of a lid covering the active site pocket |
709196 |
3.1.1.74 | more |
Pichia pastoris expressing the native non-tagged cutinase exhibits about 2- and 3fold higher values of protein amount and cutinase activity in the culture supernatant, respectively, than those containing the C-terminal tagged cutinase |
710477 |
3.1.1.74 | more |
pseudo-activation in presence of sodium bis(2-ethylhexyl)ester sulfosuccinic acid and hexadecyltrimethyl-ammoniumbromide |
208328 |
3.1.1.74 | more |
water:surfactant molar rate has a marked influence on the enzyme activity, with the best results in the range between 5 and 8. The use of detergents improves the reaction yield during wetting of cotton fibers. Increase in the stereoselectivity of the primary hydroxyl group acylation is obtained through the preincubation of the enzyme in the presence of the substrate diol 1, there is no correlation with the incubation time |
707009 |