多催化蛋白酶(prosome, proteasome):真核生物和古细菌酶的比较。

Biomedica biochimica acta Pub Date : 1991-01-01
B Dahlmann, F Kopp, L Kuehn, R Hegerl, G Pfeifer, W Baumeister
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引用次数: 0

摘要

从大鼠肌肉组织和嗜酸热原体中分离纯化的蛋白酶体具有非常相似的大小和形状,但与真核颗粒相比,古细菌中的亚基组成不那么复杂。古细菌酶含有一个具有凝乳特异性的催化位点,被丝氨酸蛋白酶抑制剂抑制,明显不同于真核粒子,真核粒子至少有三个催化位点,用于肽键水解,但机制尚不明确。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The multicatalytic proteinase (prosome, proteasome): comparison of the eukaryotic and archaebacterial enzyme.

Proteasomes isolated and purified from rat muscle tissue and from the archaebacterium Thermoplasma acidophilum have a very similar size and shape, but the subunit composition is less complex in the archaebacterium as compared to the eukaryotic particle. The archaebacterial enzyme contains a catalytic site with chymotryptic specificity, which is inhibited by serine proteinase inhibitors and clearly differs from the eukaryotic particle which has a minimum of three catalytic sites for peptide bond hydrolysis of a yet undefined mechanism.

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