Arginine substitution by alanine at the P1 position increases the selectivity of CmPI-II, a non-classical Kazal inhibitor

Arginine substitution by alanine at the P1 position increases the selectivity of CmPI-II, a non-classical Kazal inhibitor

CmPI-II is a Kazal-type tight-binding inhibitor isolated from the Caribbean snail Cenchritis muricatus. This inhibitor has an unusual specificity in the Kazal family, as it can inhibit subtilisin A (SUBTA), elastases and trypsin. An alanine in CmPI-II P1 site could avoid trypsin inhibition while imp...

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Bibliographic Details
Main Authors: Laritza Rojas, Aymara Cabrera-Muñoz, Dayrom Gil Pradas, Jessica B. González, Maday Alonso-del-Rivero, Yamile González-González
Format: Article
Language:English
Published: Elsevier 2021-07-01
Series:Biochemistry and Biophysics Reports
Subjects:
Protease
Inhibitor
Kazal-family
Site-directed mutagenesis
Subtilisin
Trypsin
Online Access:http://www.sciencedirect.com/science/article/pii/S2405580821001023

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http://www.sciencedirect.com/science/article/pii/S2405580821001023

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