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3,4‐Dichloroisocoumarin, a serine protease inhibitor, inactivates glycogen phosphorylase b
Author(s) -
Rusbridge Nicholas M.,
Bey Robert J.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80991-q
Subject(s) - glycogen phosphorylase , chemistry , serine protease , serine , biochemistry , protease inhibitor (pharmacology) , phosphorylase kinase , glycogen debranching enzyme , glycogen synthase , protease , enzyme , biology , virology , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
3,4‐Dichloroisocoumarin (3,4‐DCI) is a highly reactive, mechanism‐based inhibitor of serine proteases. We show here that glycogen phosphorylase b is also inactivated by this inhibitor, in a mechanism that parallels the inactivation of serine proteases, but involving multiple sites of covalent modification. Such a process may compromise studies in which 3,4‐DCI is used to arrest proteolysis of a second native protein which may itself be modified.