The Ligand Specificity of the (Adenosine 3',5'-Monophosphate)-Binding Site of Yeast Glyceraldehyde-3-Phosphate Dehydrogenase. Interaction with Adenosine Derivatives and Pharmacologically-Active Compounds
- 1 August 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 109 (1) , 51-59
- https://doi.org/10.1111/j.1432-1033.1980.tb04766.x
Abstract
The high-affinity cAMP-binding site of form-II baker''s yeast glyceraldehyde-3-phosphate dehydrogenase has a marked specificity for adenosine derivatives, such ligands including N6-substituted adenosine derivatives active as cytokinins in plant systems and adenine nucleotides. Of a wide range of nucleotides and nucleosides examined only adenosine derivatives bind to the cAMP binding site. A variety of antimitotic compounds (including colchicine, colcemid and phenylcarbamate derivatives), adrenergic receptor antagonists (alprenolol and propranolol) and non-steroidal antiinflammatory agents (notably indomethacin and flufenamic acid) displace cAMP from glyceraldehyde-3-phosphate dehydrogenase. Colchicine, colcemid, N6-furfuryladenosine, indomethacin, flufenamic acid and propranolol inhibit cAMP binding to the enzyme in an apparently competitive fashion. Given the evolutionary conservatism and abundance of glyceraldehyde-3-phosphate dehydrogenase, the affinity of the cAMP-binding site of this enzyme for a variety of structurally-disparate pharmacologically-active compounds compromises simple one-site interpretations of physiological responses to these agents.This publication has 35 references indexed in Scilit:
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