| Autor: |
M. Blackler, C. W. Wharton, T. Regan, S. S. Johal |
| Rok vydání: |
1995 |
| Předmět: |
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| Zdroj: |
Spectroscopy of Biological Molecules ISBN: 9789401041669 |
| Popis: |
Chymotrypsin is a serine protease. It acts selectively to catalyses the hydrolysis of peptide bonds on the C-terminus side of aromatic residues, and will also catalyse hydrolysis of hydrophobic esters such as cinnamoyl imidazole. It is composed of three polypeptide chains covalently bonded by five disulphide bridges. The molecule can be described as two cylinders of antiparallel β-sheet. Catalysis proceeds via the formation of an acyl-enzyme intermediate which can be accumulated for ester substrates. Here we present data to demonstrate the enhanced stability of an acyl-enzyme compared with two inhibitor complexes of chymotrypsin. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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