Inhibition of ribose-5-phosphate isomerase by 4-phosphoerythronate.
Hoping to exploit the special affinity of enzymes for unstable intermediates in substrate transformation, we have determined the effectiveness of possible analogs of ene-diolate intermediates as inhibitors of spinach ribose-5-phosphate isomerase. 4-Phosphoerythronic acid was found to be a very strong competitive inhibitor, with a Ki value almost 3 orders of magnitude lower than the Km value of ribose 5-phosphate, and very much lower than the Ki value of any other inhibitor that was examined.
D019747:Aldose-Ketose Isomerases; D001667:Binding, Competitive; D002238:Carbohydrate Epimerases / Q000037:antagonists & inhibitors*; D007700:Kinetics; D010944:Plants / Q000201:enzymology; D012267:Ribosemonophosphates; D013400:Sugar Acids / Q000494:pharmacology*
C020462:4-phosphoerythronate; D012267:Ribosemonophosphates; D013400:Sugar Acids; D002238:Carbohydrate Epimerases; D019747:Aldose-Ketose Isomerases; C022548:ribosephosphate isomerase