Guliaeva N V, Vul'fson P L, Severin E S
Biokhimiia. 1978 Feb;43(2):373-82.
The interaction between phosphorylase kinase (EC 2.7.1.38), isolated from rabbit skeletal muscles, and the ATP analogs with the modified triphosphate fragment: adenosine-5'-chloromethane pyrophosphonate (1), adenosine-5'-chloroethyl phosphate (2), adenosine-5'-bromethane pyrophosphonate (3), adenosine-5'-bromoethane phosphonate (4), adenosine-5'-chloroacetylaminomethane phosphonate (5), adenosine-5'-chloroacetylaminomethane pyrophosphonate (6) and adenosine-5'-chloromethane phosphonate (7), was studied. The compounds 1, 2 and 3 irreversibly inhibit the enzyme activity. In the presence of ATP the rate of inactivation is decreased. The radioactive compounds 1, 2 and 3 are stoicheometrically incorporated into the beta- and gamma-subunits of phosphorylase kinase. A correlation is shown to exist between the degree of the beta-subunit modification by compound 1 and the enzyme inactivation. The compounds 4, 5 and 6 inhibit the enzyme reversibly: in the presence of ATP complete protection of the enzyme activity is observed. The compound 7 does not affect the kinase activity; however, it binds itself to the beta-subunit of the enzyme. The binding of analogs 1 and 7 to the beta-subunit occurs at different sites. The data obtained are indicative of the catalytic role of the beta-subunit of phosphorylase kinase.
对从兔骨骼肌中分离出的磷酸化酶激酶（EC 2.7.1.38）与具有修饰三磷酸片段的ATP类似物之间的相互作用进行了研究，这些类似物包括：5'-氯甲烷焦磷酸腺苷（1）、5'-氯乙基磷酸腺苷（2）、5'-溴甲烷焦磷酸腺苷（3）、5'-溴乙烷磷酸腺苷（4）、5'-氯乙酰氨基甲烷磷酸腺苷（5）、5'-氯乙酰氨基甲烷焦磷酸腺苷（6）和5'-氯甲烷磷酸腺苷（7）。化合物1、2和3不可逆地抑制该酶的活性。在ATP存在的情况下，失活速率降低。放射性化合物1、2和3化学计量地掺入磷酸化酶激酶的β亚基和γ亚基中。显示化合物1对β亚基的修饰程度与酶失活之间存在相关性。化合物4、5和6可逆地抑制该酶：在ATP存在下观察到酶活性得到完全保护。化合物7不影响激酶活性；然而，它自身与该酶的β亚基结合。类似物1和7与β亚基的结合发生在不同位点。所获得的数据表明磷酸化酶激酶β亚基具有催化作用。
