By Wai Yiu Cheung
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Extra resources for Calcium and Cell Function
Here it was found that substitution of any of the first six residues has a profound effect on the kinetics suggesting a large active site region exists and that many interactions are important for a good fit with its substrate. Because of the likelihood of multiple interactions, it is not surprising that glycogen synthase is a reasonably good substrate. Its phosphorylatable region is very homologous to that of phosphorylase, even though it does not contain an arginyl residue on the carboxyl side of the phosphorylatable serine (Table II).
0 Â resolution and its ligand binding sites at 6 Â. J. Biol. Chem. 251, 6142. Fletterick, R. , and Madsen, N. B. (1979). Analysis of the surface topography of glycogen phosphorylase a: implications for metabolic interconversion and regulatory mechanisms. Can. J. Biochem. 57, 789. Ganapathi, M. , Silberman, S. , and Lee, E. Y. C. (1981). Dephosphorylation of rabbit skeletal muscle phosphorylase kinase. Evidence against the operation of the "sec ond-site phosphorylation" mechanism of regulation.
Biochem. 36, 95. Kohse, K. , and Heilmeyer, L. M. G. (1981). The effect of Mg 2 + on the Ca 2 + binding properties and Ca2 + -induced tyrosine-fluorescence changes of calmodulin isolated from rabbit skel etal muscle. Eur. J. Biochem. 117, 507. Krebs, E. G. (1981). Phosphorylation and dephosphorylation of glycogen phosphorylase: A pro totype for reversible covalent enzyme modification. Curr. Top. Cell. Regul. 18, 401. Krebs, E. , and Fischer, E. H. (1956). The phosphorylase b to a converting enzyme of rabbit skeletal muscle.