Dallocchio F, Matteuzzi M, Bellini T
Biochem J. 1982 May 1;203(2):401-4. doi: 10.1042/bj2030401.
Incubation of 6-phosphogluconate dehydrogenase from Candida utilis with either acetyl phosphate, 1,3-diphosphoglycerate or carbamoyl phosphate results in the phosphorylation of the protein. The binding of one phosphate residue per enzyme subunit does not affect significantly the kinetic properties, but makes the enzyme less reactive toward thiol reagents, trypsin and pyridoxal 5'-phosphate. We suggest indicate that: (1) 6-phosphogluconate dehydrogenase from C. utilis is phosphorylated non-enzymically by physiological acyl phosphates and (2) the phosphorylation of the enzyme modifies the rate of protein inactivation.
将产朊假丝酵母的6-磷酸葡萄糖酸脱氢酶与乙酰磷酸、1,3-二磷酸甘油酸或氨基甲酰磷酸一起孵育会导致该蛋白质发生磷酸化。每个酶亚基结合一个磷酸残基不会显著影响其动力学性质,但会使该酶对硫醇试剂、胰蛋白酶和磷酸吡哆醛的反应性降低。我们表明:(1)产朊假丝酵母的6-磷酸葡萄糖酸脱氢酶被生理性酰基磷酸非酶促磷酸化,以及(2)该酶的磷酸化改变了蛋白质失活的速率。