Catalytic components of the bovine pituitary multicatalytic proteinase complex (proteasome).

Enzyme & protein Pub Date : 1993-01-01 DOI:10.1159/000468687
C Cardozo
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引用次数: 38

Abstract

The multicatalytic proteinase complex (MPC), also called the proteasome, is a ubiquitous particle (19S) that is required for life. It is found in the cytoplasm and nucleus of all eukaryotic cells where it degrades selected cytosolic and nuclear proteins. It forms the proteolytic core of the 26S complex that represents the final step in the ubiquitin-dependent pathway of proteolysis. The MPC expresses at least five distinct proteolytic activities. Three activities preferring cleavages on the carboxyl side of neutral amino acids were described: an activity cleaving after branched chain residues, termed branched chain amino acid preferring, that is a major factor in the degradation of proteins, an activity preferring cleavages after bulky hydrophobic residues designated chymotrypsin-like, and an activity cleaving between small neutral amino acids. Activities cleaving after basic (trypsin-like) and acidic residues (peptidylglutamyl peptide-hydrolyzing) have also been described. The expression of multiple proteolytic activities with diverse specificities may provide a functional advantage that allows efficient hydrolysis of target proteins.

牛垂体多催化蛋白酶复合物(蛋白酶体)的催化成分。
多催化蛋白酶复合物(MPC),也称为蛋白酶体,是一种无处不在的粒子(19S),是生命所必需的。它存在于所有真核细胞的细胞质和细胞核中,在那里它降解选定的细胞质和核蛋白。它形成了26S复合物的蛋白水解核心,代表了泛素依赖的蛋白水解途径的最后一步。MPC表达至少五种不同的蛋白水解活性。描述了中性氨基酸羧基侧的三种活性裂解:支链残基后的活性裂解,称为支链氨基酸偏好,这是蛋白质降解的主要因素;大块疏水残基后的活性裂解,称为凝乳胰蛋白酶样;以及小中性氨基酸之间的活性裂解。碱性(胰蛋白酶样)和酸性残基(肽酰谷氨酰肽水解)后的裂解活性也有描述。具有不同特异性的多种蛋白水解活性的表达可能提供功能优势,允许有效水解靶蛋白。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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