Ferroni E L, Harper E T, Fife W K
Department of Chemistry, Illinois Benedictine College, Lisle 60532.
Biochem Biophys Res Commun. 1991 Apr 15;176(1):511-6. doi: 10.1016/0006-291x(91)90954-6.
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.
发现兔肌肉醛缩酶可被1-磷酸-D-赤藓酮糖以缓慢、可逆的方式灭活。该化合物能迅速且可逆地与酶结合形成初始复合物，然后该复合物仅缓慢地（一级反应速率常数ki = 0.28分钟⁻¹）转化为动力学上更稳定的形式。这种稳定的酶-配体形式对醛缩酶的正常底物1,6-二磷酸果糖无活性。然而，通过在不含1-磷酸-D-赤藓酮糖的溶液中孵育，无活性的酶-配体复合物可以分解（一级反应速率常数kr = 0.0041分钟⁻¹），再次产生活性酶。
