Protonic reorganization and substrate structure in catalysis by serine proteases
โ Scribed by Elrod, James P.; Hogg, John L.; Quinn, Daniel M.; Venkatasubban, K. S.; Schowen, Richard L.
- Book ID
- 126471480
- Publisher
- American Chemical Society
- Year
- 1980
- Tongue
- English
- Weight
- 795 KB
- Volume
- 102
- Category
- Article
- ISSN
- 0002-7863
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๐ SIMILAR VOLUMES
Isocoumarins are potent mechanism-based heterocyclic irreversible inhibitors for a variety of serine proteases. Most serine proteases are inhibited by the general serine protease inhibitor 3,4-dichloroisocoumarin, whereas isocoumarins containing hydrophobic 7-acylamino groups are potent inhibitors f
We present free energy calculations using molecular dynamics on different substrates of alpha-lytic protease in the gas phase, in solution, while forming a noncovalent Michaelis complex with the enzyme, and in a tetrahedral structure representing a transition state/intermediate for acylation by the