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Modulation of Thermolysin Activity. Reversibility of Inactivation and Superactivation
Author(s) -
Blumberg S.,
Holmquist B.,
Vallee B. L.
Publication year - 1974
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197400050
Subject(s) - chemistry , thermolysin , residue (chemistry) , enzyme , stereochemistry , biophysics , biochemistry , trypsin , biology
Chemical studies on the mechanism of the action of thermolysin implicate a histidyl residue as essential for catalysis and reveal the existence of another residue which can undergo modification with a concomitant large increase in the activity of the enzyme towards a variety of substrates.