3,4-Dichloroisocoumarin, a serine protease inhibitor, inactivates glycogen phosphorylase b.
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.
Rusbridge
N M
NM
Department of Biochemistry, University of Liverpool, UK.
Beynon
R J
RJ
D000818:Animals; D003374:Coumarins / Q000494:pharmacology*; D066298:In Vitro Techniques; D049934:Isocoumarins; D009132:Muscles / Q000201:enzymology; D006005:Phosphorylases / Q000037:antagonists & inhibitors*; D011817:Rabbits; D015842:Serine Proteinase Inhibitors
D003374:Coumarins; D049934:Isocoumarins; D015842:Serine Proteinase Inhibitors; C046235:3,4-dichloroisocoumarin; D006005:Phosphorylases