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Allosteric Regulation of Proteases
Author(s) -
Hauske Patrick,
Ottmann Christian,
Meltzer Michael,
Ehrmann Michael,
Kaiser Markus
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800528
Subject(s) - allosteric regulation , proteases , rational design , effector , small molecule , allosteric enzyme , chemistry , enzyme , protease , biochemistry , stereochemistry , nanotechnology , materials science
Abstract Allostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small‐molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. The structural bases of some proteinaceous and small‐molecule allosteric protease regulators have already been elucidated, indicating a general mechanism that might be exploitable for future rational design of small‐molecule effectors.