Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein–interface interaction: Interaction of α-chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile16–Asp194)
✍ Scribed by Fábio C. L. Almeida; Ana Paula Valente; Hernan Chaimovich
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 76 KB
- Volume
- 59
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
The stability of ␣-chymotrypsin and ␦-chymotrypsin was studied in reversed micelles of sodium bis(2ethylhexyl)sulfosuccinate (AOT) in isooctane. ␣-Chymotrypsin is inactivated at the interface and at the water pool, while ␦-chymotrypsin is inactivated only at the water pool. The mechanism of inactivation at the interface is related to the interaction of N-terminal group alanine 149 (absent in ␦-chymotrypsin) with the negative interface. The dependence of enzyme activity on water content of these two enzymes in reversed micelles of AOT is also related with the interface interaction, since ␦-chymotrypsin does not have a bell-shaped curve as observed for ␣-chymotrypsin.