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Results 1 - 10 of 26 > >>
EC Number Activating Compound Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62aprotonin 10% activation at 1 mM 754435
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62choline increases the enzyme activity 708884
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62dichloroisocoumarin - 689044
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62leupeptin 15% activation at 1 mM 754435
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62methyl-beta-cyclodextrin activates and enhances the enantioselectivity of subtilisin C. mainly by prevention of structural perturbation during the initial lyophilization process. Minor contributions to increased activity likely stem from other factors, such as, reduction of possible mass transport limitations and changes in enzyme dynamics. Enhanced activity and enantioselectivity is not caused by formation of cyclodextrin–substrate or -product complexes 688433
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62more conjugation of enzyme with comb-shaped poly-(ethylen glycol) and solubilization in ionic liquids without adding water. Enzyme exhibits higher transesterification activity in solution of [Eminm][Tf2N] than in toluene. No enzymic activity in DMSO, THF, or acetonitrile 668241
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62more dynamics are also affected by the method of preparation of the enzyme: decreased flexibility is observed when the enzyme is chemically modified with poly ethylene glycol or colyophilized with crown ethers 707804
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62more glycosylation of subtilisin does not cause any significant tertiary structure changes 707805
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62more improvement in the enzymatic activity for the poly(ethylene)-glycol-modified enzyme in the organic solvent that depends on the level of poly(ethylene)-glycolylation. PEG–SBc conjugates with 1.1, 1.9, and 3.2 average mol of poly(ethylene)-glycol per mol of protein reveal a 30fold, 57fold, and 99fold increase in enzymatic activity as a result of poly(ethylene)-glycolylation 685717
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.62more lyophilized enzyme, sharp increase in enzyme activity in correlation with an increasing amount of fumed silica added to enzyme before freeze-drying. When freezing at -20°C instead of liquid nitrogen, even better activation is observed 669901
Results 1 - 10 of 26 > >>