脂质、相互转化和蛋白水解过程对多催化蛋白酶复合物的调节。

Enzyme & protein Pub Date : 1993-01-01 DOI:10.1159/000468686
P Arizti, J Arribas, J G Castaño
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引用次数: 15

摘要

在研究多催化蛋白酶(MCP)的调节方面,我们主要集中在三个方面:(1)脂质对MCP复合物活性的调节,表明心磷脂、硫脂脂和神经节苷脂是该复合物酶活性的有效激活剂;(2)通过MCP亚基的相互转化进行调节,表明酪蛋白激酶II能够磷酸化体外复合物的C8(该亚基也是体内磷酸化的主要亚基)和C9亚基,并且26-kD亚基在体外被蛋白激酶C磷酸化;(3)通过蛋白水解加工进行调节,扩展了我们之前对C2 COOH末端蛋白水解加工的观察。在不同亚细胞组分中存在的酶活性能够通过去除C2多肽的至少最后9-13个氨基酸将完整的C2 (32kd)亚基转化为28kd多肽。所提供的数据表明,MCP复合物可能在体内受到严密的多因子控制。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Modulation of the multicatalytic proteinase complex by lipids, interconversion and proteolytic processing.

In studying the modulation of multicatalytic proteinase (MCP), we have focused on three main aspects: (1) modulation of the activity of the MCP complex by lipids, showing that cardiolipin, sulfatides and gangliosides are potent activators of the enzymatic activity of the complex; (2) modulation by interconversion of MCP subunits, showing that casein kinase II is able to phosphorylate the C8 (this subunit is also be main in vivo phosphorylated subunit) and C9 subunits of the complex in vitro and that a 26-kD subunit is phosphorylated in vitro by protein kinase C, and (3) modulation by proteolytic processing, extending our previous observation of proteolytic processing of the C2 COOH terminus, the presence of enzymatic activities in different subcellular fractions able to convert the intact C2 (32 kD) subunit to a 28-kD polypeptide by removal of at least the last 9-13 amino acids of the C2 polypeptide. The data presented illustrate that the MCP complex is probably under tight and multifactorial control in vivo.

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