Abstract
Theoretical considerations are presented for the influence of a modifier on enzyme reactions that utilize other enzymes as substrates. Activation of phosphorylase phosphatase and inhibition of phosphorylase kinase by glucose-6-P is examined. No effect of glucose-6-P could be found on alternative peptide substrates, so the effect of glucose-6-P is on the protein substrate, phosphorylase. Initial rate studies show that glucose-6-P activates phosphorylase phosphatase by increasing the VM and inhibits phosphorylase kinase by altering the binding of phosphorylase b. A comparison is given of the action of phosphorylase phosphatase on phosphorylase a and peptide substrates in attempt to determine what factors are important in substrate recognition. A preliminary study of phosphorylase kinase with peptide substrates is also given.
Supported by Research Grant GM-09587 from the National Institutes of Health, United States Public Health Service and American Heart Association Grant AHA 72-621.
Recipient of a Research Career Development Award of the United States Public Health Service, Grant GM-6753.
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Graves, D.J., Martensen, T.M., Tu, JI., Tessmer, G.M. (1974). The Use of Alternative Substrates in the Study of Phosphorylase Phosphatase and Phosphorylase Kinase. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_6
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DOI: https://doi.org/10.1007/978-3-642-80817-3_6
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