NON-ENZYMIC PROTEIN-PHOSPHORYLATION - PHOSPHORYLATION OF 6-PHOSPHOGLUCONATE DEHYDROGENASE BY ACYL PHOSPHATES
NON-ENZYMIC PROTEIN-PHOSPHORYLATION - PHOSPHORYLATION OF 6-PHOSPHOGLUCONATE DEHYDROGENASE BY ACYL PHOSPHATES
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DOI：
10.1042/bj2030401
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发表时间：
1982-01-01
影响因子：
4.1
通讯作者：
BELLINI, T
中科院分区：
文献类型：
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作者：
DALLOCCHIO, F;MATTEUZZI, M;BELLINI, T
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导致蛋白质磷酸化。每个酶亚基1个磷酸残基的结合不会显著影响动力学性质，但使酶对巯基试剂、胰蛋白酶和吡哆醛5“-磷酸的反应性降低。参与磷酸盐结合的基团可能是组氨酸残基。6-磷酸葡萄糖酸脱氢酶。utilis通过生理酰基磷酸非酶促磷酸化，并且酶的磷酸化改变蛋白质失活的速率。
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 1 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. The group involved in the binding of phosphate is probably a histidine residue. 6-Phosphogluconate dehydrogenase from C. utilis is phosphorylated non-enzymically by physiological acyl phosphates, and the phosphorylation of the enzyme modifies the rate of protein inactivation.