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.