EC Number   |
Organic Solvent |
Reference |
|---|
   3.4.21.4 | acetonitrile |
molecular dynamic simulation to study trypsin with and without a six-aminoacid peptide bound in the solvents water, acetonitrile and hexane. The enzyme is more compact and less native-like in hexane than in the other two polar solvents. The substrate can stabilize the native protein structure. There are no significant differences in the conformation of the S1 pocket upon the substrate binding in water and acetonitrile media. The substrate binding enhances the stability of catalytic H-bond network. The enzyme and the substrate appear to be more appropriate to the reactive conformation in the organic solvents compared with aqueous solution |
732354 |
| 3.4.21.4 | acetonitrile |
the presence of organic cosolvents like acetonitrile decreases the ability of boiling to completely quench trypsin activity |
699822 |
| 3.4.21.4 | guanidine-HCl |
the recombinant enzyme retains about 40 and 20% activity in 0.1 and 0.3 M guanidine-HCl |
699820 |
| 3.4.21.4 | hexane |
molecular dynamic simulation to study trypsin with and without a six-aminoacid peptide bound in the solvents water, acetonitrile and hexane. The enzyme is more compact and less native-like in hexane than in the other two polar solvents. The substrate cannot stabilize the native protein structure in the nonpolar hexane. There are no significant differences in the conformation of the S1 pocket upon the substrate binding in water and acetonitrile media while a reverse behavior is observed in hexane media, implying a possible induced fit binding mechanism in the non-polar media. The substrate binding enhances the stability of catalytic H-bond network. The enzyme and the substrate appear to be more appropriate to the reactive conformation in the organic solvents compared with aqueous solution. There is much greater substrate binding strength in hexane media than the water and acetonitrile ones |
732354 |
| 3.4.21.4 | SDS |
trypsin is denatured in the range of 2.5-3.5 mM SDS |
697444 |
| 3.4.21.4 | urea |
the recombinant enzyme retains approximately 50 and 20% of its activity in 2 and 4 M urea, respectively |
699820 |
| 3.4.21.4 | urea |
the recombinant enzyme retains approximately 80 and 50% of its activity in 2 and 4 M urea, respectively |
699820 |
