Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney leucine aminopeptidase.
Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney leucine aminopeptidase.
复制标题
金属结合化学计量和金属离子调节猪肾亮氨酸氨肽酶活性的机制。
DOI：
10.1021/bi00523a007
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Lin,SH
中科院分区：
文献类型：
--
作者：
VanWart,HE;Lin,SH
Harold E. Van Wart*和Spencer H. Lin摘要：猪肾亮氨酸氨基肽酶（Porcinekidney leucine aminopeptidase）是一种可变金属含量的非均相制剂，通过l-亮氨酸甘氨酸- ah - sepharose亲和层析纯化。用Zn2+处理后再进行凝胶过滤，恢复了天然酶的Zn2+含量，每个六聚体的Zn2+含量为6 mol，每个六聚体位于每个亚基的单个催化结合位点。用二价金属离子孵育可调节天然酶的活性；它是被激活的i -尿氨酸氨基肽酶（LAP） 1 （EC 3.4）。11.1)是锌金属肽酶中的一种，参与多肽和蛋白质的代谢（Himmelhoch, 1970; Delange & Smith, 1971）。锌金属肽酶通常又分为内肽酶，如热溶酶；c端外肽酶，如羧基肽酶A和B； n端肽酶，如亮氨酸氨基肽酶。从前两类酶中，热溶素和羧肽酶A在其晶体结构和动力学方面得到了广泛的研究
Harold E. Van Wart* and Spencer H. Lin abstract: Porcinekidney leucine aminopeptidase has been obtained from commercial sources as an inhomogeneous preparation with variable metal content and purified by affinity chromatography over L-leucylglycyl-AH-Sepharose. Treat-ment· with Zn2+ followed by gel filtration restores the Zn2+ content of the native enzyme, which is 6 mol of Zn2+ per hexamer, each of which is located at a single catalytic binding site per subunit. The activity of the native enzyme is modulated by incubation with divalent metal ions; it is activatedI-Veucine aminopeptidase (LAP) 1 (EC 3.4. 11.1) is one of a broad class of zinc metallopeptidases that is involved in the metabolism of peptides and proteins (Himmelhoch, 1970; Delange & Smith, 1971). Zinc metallopeptidases are usually subdivided into the endopeptidases, such as thermolysin, the C-terminal exopeptidases, such as carboxypeptidases A and B, and the N-terminal peptidases, such as leucine amino-peptidase. From the former two classes of enzymes, thermolysin and carboxypeptidase A have been extensively studied with respect to both their crystalstructures and their kinetic