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首页> 外文期刊>Parasitology >Molecular cloning and characterization of a M17 leucine aminopeptidase of Cryptosporidium parvum
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Molecular cloning and characterization of a M17 leucine aminopeptidase of Cryptosporidium parvum

机译：细小隐孢子虫M17亮氨酸氨基肽酶的分子克隆与表征

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摘要

Leucine aminopeptidases (LAPs) are a group of metalloexopeptidases that catalyse the sequential removal of amino acids from the N-termini of polypeptides or proteins. They play an important role in regulating the balance between catabolism and anabolism in living cells. LAPs of apicomplexa parasitic protozoa have been intensively investigated due to their crucial roles in parasite biology as well as their potentials as drug targets. In this study, we identified an M17 leucine aminopeptidase of Cryptosporidium parvum (CpLAP) and characterized the biochemical properties of the recombinant protein. Multiple sequence alignment of the deduced amino acid sequence of CpLAP with those of other organisms revealed that typical amino acid residues essential for metal binding and active-site formation in M17 LAPs were well conserved in CpLAP. Recombinant CpLAP shared similar biochemical properties such as optimal pH, stability at neutral pHs, and metal-binding characteristics with other characterized LAPs. The enzyme showed a marked preference for Leu and its activity was effectively inhibited by bestatin. These results collectively suggest that CpLAP is a typical member of the M17 LAP family and may play an important role in free amino acid regulation in the parasite.
机译：亮氨酸氨基肽酶（LAPs）是一组金属肽酶，其催化从多肽或蛋白质的N-末端连续去除氨基酸。它们在调节活细胞分解代谢和合成代谢之间的平衡中起重要作用。由于其在寄生虫生物学中的关键作用及其作为药物靶标的潜力，对蜂复合体寄生原生动物的LAP进行了深入研究。在这项研究中，我们鉴定了小隐隐孢子虫（CpLAP）的M17亮氨酸氨基肽酶，并表征了重组蛋白的生化特性。 CpLAP推导的氨基酸序列与其他生物的氨基酸序列的多序列比对显示，Mp17 LAP中金属结合和活性位点形成所必需的典型氨基酸残基在CpLAP中保存良好。重组CpLAP与其他特征性LAP具有相似的生化特性，例如最佳pH，在中性pH下的稳定性以及金属结合特性。该酶显示出对Leu的显着偏好，其活性被Bestatin有效抑制。这些结果共同表明，CpLAP是M17 LAP家族的典型成员，并且可能在寄生虫的游离氨基酸调节中发挥重要作用。

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