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Insights from the in silico structural, functional and phylogenetic characterization of canine lysyl oxidase protein.
Journal of Genetic Engineering and Biotechnology Pub Date : 2020-06-16 , DOI: 10.1186/s43141-020-00034-w
Afnan Saleem 1 , Shiveeli Rajput 2
Affiliation  

Lysyl oxidase is an extracellular regulatory enzyme with an imperative role in interlinking of collagen and elastin by oxidizing lysine residues. Lysyl oxidase has been implicated in incidence of mammary tumors in bitches. Therefore, it becomes significant to study the structural and functional features of this enzyme for a better understanding of its molecular mechanisms. The detailed computational investigation of the canine lysyl oxidase protein was analyzed in silico with respect to its physicochemical properties, secondary and tertiary structure predictions and functional analysis using standard bioinformatic tools. Lysyl oxidase is a flexible protein with an average molecular weight of around 46 kDa, unstable, hydrophilic, and extracellular (secretory) in nature. Twelve cysteine residues and a disulfide bridge were also found. Secondary structure analysis shows that most of the protein has predominant coiled configuration. A putative copper-binding region signature was predicted. The phylogenetic relationship of canine lysyl oxidase with a vast range of mammalian species indicates that the protein was very well conserved throughout the course of evolution. Top 10 interacting proteins were identified using STRING v10.0 analysis, elastin being the closest interacting protein. Functional analysis by InterproScan predicted protein’s biological role in oxidation-reduction process. Understanding the structural and functional properties of the protein will facilitate a better understanding of its mechanism of enzyme action. Further, the predicted 3D model will serve as a cornerstone for further understanding towards the tumorigenesis potential of the protein.

中文翻译:

从犬赖氨酰氧化酶蛋白的计算机结构,功能和系统发育特征中获得的见解。

赖氨酰氧化酶是一种细胞外调节酶,通过氧化赖氨酸残基在胶原蛋白和弹性蛋白的相互连接中起着至关重要的作用。赖氨酰氧化酶已被认为与母犬的乳腺肿瘤有关。因此,研究该酶的结构和功能特征以更好地了解其分子机理变得很重要。使用标准生物信息学工具,通过计算机分析了犬赖氨酰氧化酶蛋白的详细计算研究,包括其理化性质,二级和三级结构预测以及功能分析。赖氨酰氧化酶是一种灵活的蛋白质,平均分子量约为46 kDa,性质不稳定,亲水且具有细胞外(分泌)功能。还发现了十二个半胱氨酸残基和二硫键。二级结构分析表明,大多数蛋白质具有主要的卷曲构型。预测了铜结合区的特征。犬赖氨酰氧化酶与广泛的哺乳动物物种的系统发育关系表明该蛋白在整个进化过程中都非常保守。使用STRING v10.0分析确定了前10个相互作用蛋白,弹性蛋白是最接近的相互作用蛋白。InterproScan进行的功能分析预测了蛋白质在氧化还原过程中的生物学作用。了解蛋白质的结构和功能特性将有助于更好地了解其酶作用机制。此外,预测的3D模型将作为进一步了解该蛋白的致瘤潜力的基石。
更新日期:2020-06-16
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