Plant Molecular Biology Unit, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411 008, Maharashtra, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, Uttar Pradesh, India.
Plant Molecular Biology Unit, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411 008, Maharashtra, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, Uttar Pradesh, India.
Biochim Biophys Acta Gen Subj. 2020 Dec;1864(12):129703. doi: 10.1016/j.bbagen.2020.129703. Epub 2020 Aug 15.
α-Amylase inhibitors (α-AIs) belong to the discrete classes, and exhibited differential specificities against α-amylases from various sources. Several α-amylases and their complexes with inhibitors at the molecular level have been studied in detail. Interestingly, some α-AIs depict specific and selective interactions amid different insect α-amylases.
There are studies to understand evolutionary variability and functional differentiation of insect α-amylases and their cognate inhibitors. We have examined sequence, structural, and interaction diversity between various α-amylases and α-AIs. Based on these analyses, we are providing a potential basis for the functional differentiation among certain insect α-amylases concerning mammalian counterparts and their interactions with different proteinaceous α-AIs.
Insect α-amylases have conserved domain architecture with differences in length, number of disulfide bonds, and secondary structure. Furthermore, few of them exhibit variable characteristics like chloride dependent activity, the presence of N-terminal glutamine residue to protect against proteolytic degradation, and loop variations near the enzyme active site. Conformation of α-AI protein could be an essential factor for their specificity and binding affinities towards target α-amylase(s). Furthermore, variation into the enzyme binding pocket residues might contribute to differential interactions with inhibitors.
Molecular insights in the interactions between insect α-amylases and plant α-AI will provide the details of mechanisms assisting the inhibitor specificity. Furthermore, this information will help to design potent and effective α-AIs against specific α-amylase.
α-淀粉酶抑制剂（α-AIs）属于离散类，对来自不同来源的α-淀粉酶表现出不同的特异性。已经在分子水平上对几种α-淀粉酶及其与抑制剂的复合物进行了详细研究。有趣的是，一些α-AIs 在不同昆虫α-淀粉酶之间表现出特定和选择性的相互作用。
有研究旨在了解昆虫α-淀粉酶及其同源抑制剂的进化可变性和功能分化。我们检查了各种α-淀粉酶和α-AIs 之间的序列、结构和相互作用多样性。基于这些分析，我们为某些昆虫α-淀粉酶与哺乳动物对应物之间的功能分化以及它们与不同蛋白α-AIs 的相互作用提供了潜在的基础。
昆虫α-淀粉酶具有保守的结构域架构，但在长度、二硫键数量和二级结构方面存在差异。此外，它们中的一些具有可变特征，如氯离子依赖的活性、存在 N 端谷氨酰胺残基以防止蛋白水解降解以及酶活性位点附近的环变化。α-AI 蛋白的构象可能是其对靶标α-淀粉酶（s）特异性和结合亲和力的重要因素。此外，酶结合口袋残基的变化可能有助于与抑制剂的差异相互作用。
昆虫α-淀粉酶和植物α-AI 之间相互作用的分子见解将提供有助于抑制剂特异性的机制细节。此外，这些信息将有助于设计针对特定α-淀粉酶的有效和有效的α-AIs。
