Enhanced proteolysis of glucose-6-phosphate dehydrogenase in the presence of palmitoyl coenzyme A.
Palmitoyl coenzyme A at concentrations below its critical micelle concentration increases the rate of proteolysis of baker's yeast glucose-6-phosphate dehydrogenase by proteinase A in the pH range 4-5. both glucose-6-phosphate and NADP protect glucose-6-phosphate dehydrogenase against proteolysis, but these protective effects are diminished in the presence of palmitoyl coenzyme A. Since palmitoyl coenzyme A is known to dissociate glucose-6-phosphate dehydrogenase into dimers, the results imply that the in vivo half life of glucose-6-phosphate dehydrogenase may be controlled by a process based on the regulation of the oligomeric structure of the enzyme by the collective actions of various molecules, including palmitoyl coenzyme A.
Orstan
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Institute of Gerontology, University of Michigan, Ann Arbor 48109-2007.
Gafni
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D016282:Aspartic Acid Endopeptidases / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010171:Palmitoyl Coenzyme A / Q000378:metabolism* / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013050:Spectrometry, Fluorescence
D005656:Fungal Proteins; D010171:Palmitoyl Coenzyme A; D005954:Glucosephosphate Dehydrogenase; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases