Slow reversible inhibition of rabbit muscle aldolase by D-erythrulose 1-phosphate

Abstract

Rabbit muscle aldolase was found to be inactivated in a slow, reversible manner by D-erythrulose 1-phosphate. This compound combined rapidly and reversibly with the enzyme to form an initial complex, which then only slowly (k i = 0.28 min −1) converted to a kinetically more stable form. This stable enzyme-ligand form was inactive toward the normal substrate of aldolase, fructose 1,6-bisphosphate. The inactive enzyme-ligand complex, however, could be decomposed (k r = 0.0041 min −1) to yield active enzyme once again by incubation in a solution devoid of D-erythrulose 1-phosphate.