嘌呤和甘油对牛脑低分子量酸性磷酸酶的激活作用。

Activation of low molecular weight acid phosphatase from bovine brain by purines and glycerol.

作者信息

Tanizaki M M, Bittencourt H M, Chaimovich H

出版信息

Biochim Biophys Acta. 1977 Nov 23;485(1):116-23. doi: 10.1016/0005-2744(77)90198-x.

PMID:199263

Abstract

Low molecular weight acid phosphatase (orthophosphoric monoester phosphophydrolase (acid optimum), EC 3.1.3.2) from bovine brain is activated up to 4-fold by guanosine, guanine, adenine, adenosine, and 6-ethylmercapto-purine. Several pyrimidines and other purines were tested and did not show any activation effect. The rate enhancement induced by purines is uncompetitive and not caused by transphosphorylation to the activator. Using transphosphorylation to glycerol as a probe, it is proposed that the activator binds to one of the phosphorylated intermediates in the reaction pathway. These findings are discussed in terms of the catalytic mechanism of low molecular weight acid phosphatase.

摘要

来自牛脑的低分子量酸性磷酸酶（正磷酸单酯磷酸水解酶（最适酸性），EC 3.1.3.2）被鸟苷、鸟嘌呤、腺嘌呤、腺苷和6-乙基巯基嘌呤激活至4倍。测试了几种嘧啶和其他嘌呤，未显示任何激活作用。嘌呤诱导的速率增强是非竞争性的，不是由向激活剂的转磷酸化引起的。以向甘油的转磷酸化为探针，提出激活剂与反应途径中的一种磷酸化中间体结合。根据低分子量酸性磷酸酶的催化机制对这些发现进行了讨论。