Abstract
Rabbit skeletal muscle phosphorylase kinase exists in two kinetically different forms (1). One of these forms, referred to as nonactivated phosphorylase kinase, has very little activity at pH 6.8 and is only partially active at higher pH values. The other form of the enzyme, activated phosphorylase kinase, is highly active at pH 6.8 and at pH 8.2. Conversion of nonactivated phosphorylase kinase to the activated form can be brought about in vitro by limited proteolysis (2, 3) or as a result of phosphorylation by ATP. It is doubtful whether the first type of activation is of physiological significance, but it seems very likely that activation by ATP does constitute a meaningful regulatory device. Phosphorylation and activation of the muscle kinase is accelerated by cyclic AMP (1, 4, 5); moreover, it has been possible to correlate the activation of the enzyme with changes in the cyclic AMP concentration produced by epinephrine administration in vivo (6). A further indication that phosphorylation and activation of phosphorylase kinase actually occurs in muscle is the fact that this tissue contains a phosphatase capable of reversing the process (7). Many of the properties noted for the skeletal muscle enzyme have also been observed with heart muscle phosphorylase kinase (8–10).
Supported by Grant AM 12842 from the U.S. Public Health Service and a Grant-in-Aid from the American Heart Association.
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References
Krebs, E. G., Graves, D. J., and Fischer, E. H., J. Biol. Chem., 234, 2867 (1959).
Meyer, W. L., Fischer, E. H., and Krebs, E. G., Biochemistry, 3, 1033 (1964).
Huston, R. B. and Krebs, E. G., Biochemistry, 7, 2116 (1968).
Krebs, E. G., Love, D. S., Bratvold, G. E., Trayser, K. A., Meyer, W. L., and Fischer, E. H., Biochemistry, 3, 1022 (1964).
DeLange, R. J., Kemp, R. G., Riley, W. D., Cooper, R. A., and Krebs, E. G., J. Biol. Chem., 243, 2200 (1968).
Posner, J. B., Stern, R., and Krebs, E. G., J. Biol. Chem., 240, 982 (1965).
Riley, W. D., DeLange, R. J., Bratvold, G. E., and Krebs, E. G., J. Biol. Chem. 243, 2209 (1968).
Hammermeister, K. E., Yunis, A. A., and Krebs, E. G., J. Biol. Chem., 240, 986 (1965).
Drummond, G. I., and Duncan, L., J. Biol. Chem., 241, 3097 (1966).
Drummond, G. I., Duncan, L., and Friesen, A. J. D., J. Biol. Chem., 240, 2778 (1965).
Ozawa, E., Hosoi, K., and Ebashi, S., J. Biochem., 61, 531 (1967).
Brostrom, C. O., Hunkeler, F. L., and Krebs, E. G., J. Biol. Chem., 246, 1961 (1971).
Heilmeyer, L. M. G., Meyer, F., Haschke, R. H., and Fischer, E. H., J. Biol. Chem. 245, 6649 (1970).
Villar-Palasi, C., and Wei, S. I., Proc. Nat. Acad. Sci. U.S., 67, 345, (1970).
Drummond, G. I., Harwood, J. P., and Powell, C. A., J. Biol. Chem., 244, 4235 (1969).
Mayer, S. E., Namm, D. H., and Hickenbottom, J. P., Adv. in Enz. Reg., 8, 205 (1970).
Meyer, F., Heilmeyer, L. M. G., Haschke, R. H., and Fischer, E. H., J. Biol. Chem., 245, 6642 (1970).
Hayakawa, T., Perkins, J. P., Walsh, D. A., and Krebs, E. G., Unpublished results.
Hayakawa, T., Perkins, J. P., and Krebs, E. G., Unpublished results.
Walsh, D. A., Perkins, J. P., and Krebs, E. G., J. Biol. Chem., 243, 3763 (1968).
Walsh, D. A., Perkins, J. P., Brostrom, C. O., Ho, E. S., and Krebs, E. G., J. Biol. Chem., 246, 1968 (1971).
Walsh, D. A., Ashby, C. D., Gonzales, C., Calkins, D., Fischer, E. H., and Krebs, E. G., J. Biol. Chem., 246, 1977 (1971).
Sohlender, K. K., Wei, S. H., and Villar-Palasi, C, Biochim. Biophys. Acta, 191, 272 (1969).
Soderling, T. R., Hickenbottom, J. P., Reimann, E. M., Hunkeler, F. L., Walsh, D. A., and Krebs, E. G., J. Biol. Chem., 245, 6317 (1970).
Corbin, J. D., Reimann, E. M., Walsh, D. A., and Krebs, E. G., J. Biol. Chem., 245, 4849 (1970).
Huttunen, J. K., Steinberg, D., and Mayer, S. E., Proc. Nat. Acad. Sci. U.S., 67, 290 (1970).
Kuo, J. F., and Greengard, P., Proc. Nat. Acad. Sci. U.S., 64, 1349 (1969).
Kuo, J. F., and Greengard, P., J. Biol. Chem., 244, 3417 (1969).
Brostrom, M. A., Reimann, E. M., Walsh, D. A., and Krebs, E. G., Adv. in Enz. Reg., 8, 191 (1970).
Gill, G. N., and Garren, L. D., Biochem. Biophys. Res. Commun., 39, 335 (1970).
Tao, M., Salas, M. L., and Lipmann, F., Proc. Nat. Acad. Sci. U.S., 67, 408 (1970).
Kumon, A., Yammamura, H., and Nichizuka, Y., Biochem. Biophys. Res. Commun., 41, 1290 (1970).
Reimann, E. M., Brostrom, C. U., Corbin, J. D., King, C. A., and Krebs, E. G., Biochem. Biophys. Res. Commun., 42, 187 (1971).
Erlichman, J., Hirsch, A. H., and Rosen, O. M., Proc. Nat. Acad. Sci. U.S., 68, 731 (1971).
Majumder, G. C., and Turkington, R. W., J. Biol. Chem. 246, 2650 (1971).
Reimann, E. M., Walsh, D. A., and Krebs, E. G., J. Biol. Chem., 246, 1986 (1971).
Miyamoto, E., Petzold, G. L., Harris, J. S., and Greengard, P., Biochem. Biophys. Res. Commun., 44, 305 (1971).
Chen, L. J., and Walsh, D. A., Biochemistry, 0, 3614 (1971).
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Krebs, E.G., Beavo, J.A., Brostrom, C.O., Corbin, J.D., Hayakawa, T., Walsh, D.A. (1972). The Mechanism of Action of Cyclic AMP in the Activation of Phosphorylase Kinase. In: Wieland, O., Helmreich, E., Holzer, H. (eds) Metabolic Interconversion of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-37966-0_9
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