Pal Siddhartha, Sengupta Kriti
National Centre for Cell Science, Ganeshkhind, Pune, 411007 India.
Bioenergy Group, Agharkar Research Institute, Gopal Ganesh Agarkar Road, Pune, 411004 India.
3 Biotech. 2020 Sep;10(9):391. doi: 10.1007/s13205-020-02388-x. Epub 2020 Aug 14.
Alkane-1-monooxygenase of alkanotrophic species has been characterized using standard bioinformatics tools to investigate phylogenetic relationships, and three-dimensional structure and functions. Results revealed that activity of the alkane-1-monooxygenase would be optimum in alkaline pH as their isoelectric points were in the range of 7.5 to 9. Higher aliphatic index (87 to 95) indicated that these enzymes are thermostable. Extinction coefficient of the enzyme varied from 68,793 to 1,25,820 M cm and average molecular weight was 45 kDa. Secondary structures predicted maximum alpha-helical content rather than the other conformations such as sheets or turns. The instability index (II) of most stable query protein was 39.7% which was lowest among all 76 proteins analysed in this study. Predicted 3D structure of query protein revealed that it contains homodimer polypeptides. The suitable template for query protein was Flavin-dependent luciferase-type alkane monooxygenase. The presence of 98.3% amino acid residues in Ramachandran plot was determined in 3-D protein model which confirmed the model feasibility. The predicted model contains 12% more α-helix than template protein which indicated towards membrane localization of the protein. The protein interactome partners of predicted model were determined as FMN-dependent oxidoreductase, molybdopterin, nuclear transport factor, and peroxiredoxin. The predicted tertiary model of alkane-1-monooxygenase (OOL33526.1) was deposited in Protein Model Database (Accession No.: PM0083166). The overall report is unique to best of our knowledge, and the importance of this study is to understand the theoretical aspects of structure and functions of alkane-1-monooxygenase of hydrocarbonoclastic strains of .
已使用标准生物信息学工具对嗜烷物种的烷烃-1-单加氧酶进行了表征，以研究系统发育关系、三维结构和功能。结果表明，烷烃-1-单加氧酶的活性在碱性pH下最佳，因为它们的等电点在7.5至9的范围内。较高的脂肪族指数（87至95）表明这些酶是耐热的。该酶的消光系数在68,793至125,820 M⁻¹cm⁻¹之间变化，平均分子量为45 kDa。二级结构预测最大的α-螺旋含量，而不是其他构象，如片层或转角。最稳定的查询蛋白的不稳定指数（II）为39.7%，在本研究分析的所有76种蛋白中是最低的。查询蛋白的预测三维结构表明它包含同型二聚体多肽。查询蛋白的合适模板是黄素依赖性荧光素酶型烷烃单加氧酶。在三维蛋白质模型中确定了拉氏图中98.3%的氨基酸残基，这证实了模型的可行性。预测模型比模板蛋白多包含12%的α-螺旋，这表明该蛋白定位于膜上。预测模型的蛋白质相互作用组伙伴被确定为FMN依赖性氧化还原酶、钼蝶呤、核转运因子和过氧化物酶。烷烃-1-单加氧酶（OOL33526.1）的预测三级模型已存入蛋白质模型数据库（登录号：PM0083166）。据我们所知，总体报告是独一无二的，本研究的重要性在于了解烃类分解菌株的烷烃-1-单加氧酶的结构和功能的理论方面。
