Abstract
5′AMP is known to be the most efficient activator of glycogen phosphorylase b. We have compared its effects on this enzyme with those of some analogs modified in the adenine moiety or of adenine, adenosine and ATP. These effects are connected with specific steps of the chemical relaxation spectrum of phosphorylase b. The analogs are therefore very useful in order to establish a plausible scheme of the enzymatic transconformations which finally lead to a state of high affinity for substrates.
On leave of absence from Departamento Quimica-Fisica, Universidad Complutense, Madrid, Spain. Recipient of a long term EMBO fellowship.
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Abbreviations
- 5′AMP:
-
adenosine-5′-monophosphate
- SHMP:
-
6-mercaptopurine 5′-monophosphate
- 2APRMP:
-
2-amino-purine-5′monophosphate
- IMP:
-
hypoxanthine-riboside- 5′-monophosphate
- DTNB:
-
5,5′-dithiobis- (2-Nitrobenzoic acid)
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Buc, H., Buc, M.H., Blanco, F.G., Morange, M., Winkler, H. (1974). Role of 5′AMP and of Its Analogs in the Activation of Muscle Glycogen Phosphorylase b . In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_3
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DOI: https://doi.org/10.1007/978-3-642-80817-3_3
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