Type of Document	Dissertation
Author	Lanciotti, Robert Arthur
URN	etd-06062008-163955
Title	Baculovirus-directed expression of the phosphorylase kinase catalytic subunit :pseudosubstrate and calmodulin regulation
Degree	PhD
Department	Biochemistry and Anaerobic Microbiology
Advisory Committee	Advisor Name Title Bender, Patrick K. Committee Chair Bevan, David R. Committee Member Kennelly, Peter J. Committee Member Lederman, Muriel Committee Member Potts, Malcolm Committee Member
Keywords	Calmodulin
Date of Defense	1994-08-05
Availability	restricted
Abstract Phosphorylase kinase (EC 2.7.1.38) is a key enzyme involved in the regulation of the glycogenolysis pathway. It catalyzes the Ca2+ -dependent phosphorylation and activation of the enzyme glycogen phosphorylase to make the active form glycogen phosphorylase. Phosphorylase kinase is composed of 4 subunits with a stoichiometry of (αβγδ)4. The γ subunit is the catalytic subunit. The regulatory domain (residues 277-387) of γ contains a sequence resembling the sites phosphorylated in known γ substrates with the exception that a valine332 occurs at the analogous position of the phosphorylated serine or threonine residue.
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