Slow reversible inhibition of rabbit muscle aldolase by D-erythrulose 1-phosphate.
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 (ki = 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 (kr = 0.0041 min-1) to yield active enzyme once again by incubation in a solution devoid of D-erythrulose 1-phosphate.
Ferroni
E L
EL
Department of Chemistry, Illinois Benedictine College, Lisle 60532.
Harper
E T
ET
Fife
W K
WK
D000818:Animals; D001667:Binding, Competitive; D005634:Fructose-Bisphosphate Aldolase / Q000037:antagonists & inhibitors*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D011485:Protein Binding; D011817:Rabbits; D013379:Substrate Specificity; D013403:Sugar Phosphates / Q000378:metabolism / Q000494:pharmacology*
D013403:Sugar Phosphates; C068308:erythrulose 1-phosphate; D005634:Fructose-Bisphosphate Aldolase