Proline-dependent structural and biological properties of peptides and proteins.
Proline-dependent structural and biological properties of peptides and proteins.
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DOI：
10.3109/10409239309082572
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发表时间：
1993
影响因子：
6.5
通讯作者：
A. Yaron;F. Naider
中科院分区：
文献类型：
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作者：
A. Yaron;F. Naider
脯氨酸残基赋予肽链独特的结构约束，并显著影响近端肽键对蛋白酶活性的敏感性。这篇综述提出了一个关键的分析肽酶参与裂解含有脯氨酸肽键，特别注意脯氨酸肽酶在生物活性肽的寿命调节中的作用。所讨论的肽酶包括氨肽酶P、脯氨酸酶、二肽基肽酶IV、脯氨酸内肽酶和脯氨酸亚胺肽酶。HIV-1蛋白酶也受到关注，因为这种关键酶处理Xaa-Pro肽键。对上述酶的分析表明，它们可能是控制许多肽激素活性的关键起搏器，并参与多种免疫过程，包括t细胞介导的免疫反应。本文综述了Xaa-Pro键顺反异构化的新发现以及肽基脯氨酸顺反异构酶（亲免疫蛋白）的生物学功能。
Proline residues confer unique structural constraints on peptide chains and markedly influence the susceptibility of proximal peptide bonds to protease activity. This review presents a critical analysis of peptidases involved in the cleavage of proline-containing peptide bonds, with particular attention to the role of proline peptidases in the regulation of the lifetime of biologically active peptides. Peptidases discussed include aminopeptidase P, prolidase, dipeptidyl peptidase IV, prolyl endopeptidase, and prolyl iminopeptidase. Attention is also given to HIV-1 protease, because this key enzyme processes an Xaa-Pro peptide bond. Analysis of the above enzymes reveals that they may function as key pacemakers in the control of the activity of many peptide hormones and that they are involved in a variety of immunological processes, including T-cell-mediated immune response. The novel occurrence of cis-trans isomerization about Xaa-Pro bonds and the biological function of peptidyl-prolyl cis-trans isomerases (immunophilins) are reviewed.