Slow reversible inhibition of rabbit muscle aldolase by D-erythrulose 1-phosphate |
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Authors: | E L Ferroni E T Harper W K Fife |
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Institution: | Department of Chemistry, Illinois Benedictine College, Lisle 60532. |
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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 (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. |
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