The family of M17 aminopeptidases (alias 'leucine aminopeptidases', M17-LAPs) utilize a highly conserved hexameric structure and a binuclear metal center to selectively remove N-terminal amino acids from short peptides. However, M17-LAPs are responsible for a wide variety of functions that are seemingly unrelated to proteolysis. Herein, we aimed to investigate the myriad of functions attributed to M17. Further, we attempted to differentiate between the different molecular mechanisms that allow the conserved hexameric structure of an M17-LAP to mediate such diverse functions. We have provided an overview of research that identifies precise physiological roles of M17-LAPs, and the distinct mechanisms by which the enzymes moderate those roles. The review shows that the conserved hexameric structure of the M17-LAPs has an extraordinary capability to moderate different molecular mechanisms. We have broadly categorized these mechanisms as 'aminopeptidase-based', which include the characteristic proteolysis reactions, and 'association-driven', which involves moderation of the molecule's macromolecular assembly and higher order complexation events. The different molecular mechanisms are capable of eliciting very different cellular outcomes, and must be regarded as distinct when the physiological roles of this large and important family are considered.

中文翻译：

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M17氨基肽酶通过调节其大分子装配和活性位点环境来使功能多样化。

M17氨基肽酶家族（别名为“亮氨酸氨基肽酶”，M17-LAPs）利用高度保守的六聚体结构和双核金属中心从短肽中选择性去除N末端氨基酸。但是，M17-LAP负责似乎与蛋白水解无关的多种功能。在此，我们旨在研究归因于M17的众多功能。此外，我们试图区分允许M17-LAP保守的六聚体结构介导这种不同功能的不同分子机制。我们提供了确定M17-LAPs的确切生理作用以及酶调节这些作用的独特机制的研究概述。审查表明，M17-LAPs的保守六聚体结构具有调节不同分子机制的非凡能力。我们将这些机制大致归类为“基于氨基肽酶的机制”和“缔合驱动的”，其中包括基于特征的蛋白水解反应和“缔合驱动的”，其中涉及分子大分子组装的缓和和更高阶的络合事件。不同的分子机制能够引发非常不同的细胞结果，因此，当考虑到这个重要的大家族的生理作用时，必须将其视为不同的分子机制。这涉及到分子大分子组装的缓和和更高阶的络合事件。不同的分子机制能够引发非常不同的细胞结果，因此，当考虑到这个重要的大家族的生理作用时，必须将其视为不同的分子机制。这涉及到分子大分子组装的缓和和更高阶的络合事件。不同的分子机制能够引发非常不同的细胞结果，并且当考虑到这个重要的大家族的生理作用时，必须将其视为不同的。