Inhibition of proteinase K by phosphorylated sugars.
Proteolysis of lactate dehydrogenase, aldolase and the synthetic substrate N-succinylalanylalanylalanyl-p-nitroanilide by proteinase K is inhibited by glucose-6-phosphate and fructose-1,6-biphosphate. Analysis of the kinetic data obtained with the synthetic substrate indicates that the inhibition is a mixed-type and that more than one inhibitor molecule binds to proteinase K. Glucose and fructose are ineffective as inhibitors. In the presence of 0.2-4 mM fructose-1,6-biphosphate, aldolase becomes more susceptible to proteolysis, probably as a result of a conformational change induced by the substrate.
Orstan
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Institute of Gerontology, University of Michigan, Ann Arbor 48109-2007.
Gafni
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D000595:Amino Acid Sequence; D000818:Animals; D002241:Carbohydrates / Q000737:chemistry / Q000494:pharmacology*; D019286:Endopeptidase K; D005634:Fructose-Bisphosphate Aldolase; D066298:In Vitro Techniques; D007700:Kinetics; D007770:L-Lactate Dehydrogenase; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010766:Phosphorylation; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity
D002241:Carbohydrates; D009842:Oligopeptides; C015516:succinyl-trialanine-4-nitroanilide; D007770:L-Lactate Dehydrogenase; D012697:Serine Endopeptidases; D019286:Endopeptidase K; D005634:Fructose-Bisphosphate Aldolase