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主管单位 工业和信息化部 主办单位 哈尔滨工业大学 主编 任南琪 国际刊号ISSN 1672-5565 国内刊号CN 23-1513/Q

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引用本文:齐燕姣,陆会宁,金能智,赵娅敏.α-葡萄糖苷酶与米格列醇相互作用及其进化关系[J].生物信息学,2015,13(3):141-149.
QI Yanjiao,LU Huining,JIN Nengzhi,ZHAO Yamin.Interaction and evolutional analysis of α-glucosidases and Miglitol[J].Chinese Journal of Bioinformatics,2015,13(3):141-149.
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α-葡萄糖苷酶与米格列醇相互作用及其进化关系
齐燕姣1,陆会宁2,金能智3,赵娅敏1
(1. 西北民族大学榆中校区化工学院, 兰州 730124;2. 西北民族大学榆中校区生命科学与工程学院, 兰州 730124;3. 甘肃省计算中心, 兰州 730000)
摘要:
用生物信息学的方法分析不同物种的α-葡糖糖苷酶的亲缘关系,分析降血糖药物米格列醇与甜菜(Beta vulgaris)的α-葡糖糖苷酶相互作用位点在其他亲缘关系较近的物种中相应的氨基酸变化特点,结果表明米格列醇位于一个凹向酶分子内部的狭窄的结合口袋中,其间的相互作用主要以静电相互作用、氢键和范德华力为主。由于米格列醇的强水溶性和多羟基的特点,与酸性的天冬氨酸之间形成多个Ο-Η氢键,对甜菜(Beta vulgaris)的α-葡萄糖苷酶具有较好的抑制作用。通过TMHMM预测甜菜(Beta vulgaris)的α-葡萄糖苷酶的序列,结果未发现跨膜区。通过多序列比对发现,在米格列醇与甜菜(Beta vulgaris)的α-葡萄糖苷酶相互作用位点处的氨基酸中,在与其亲缘关系较近的5个物种茶(Camellia sinensis),黄瓜(Cucumis sativus),木本棉(Gossypium arboretum),甘庶属割手密(Spontaneum)和蒺藜状苜蓿(Medicago truncatula)中有81.82%的氨基酸都是保守的,且主要是极性的氨基酸,如色氨酸和天冬氨酸。这为进一步研究降血糖药物在其他物种中的表现及相互作用提供了重要的科学依据。
关键词:  α-葡萄糖苷酶  相互作用  序列比对  系统发育关系
DOI:10.3969/j.issn.1672-5565.2015.03.01
分类号:TP925+.4
基金项目:
Interaction and evolutional analysis of α-glucosidases and Miglitol
QI Yanjiao1,LU Huining2, JIN Nengzhi3,ZHAO Yamin1
(1. Department of Chemical Engineering, Northwest University for Nationalities, Lanzhou 730124, China;2. Department of Life Science and Biological Engineering, Northwest University for Nationalities, Lanzhou 730124, China;3. Gansu Province Computing Center, Lanzhou 730000, China)
Abstract:
The phylogenetic relationship of α-glucosidase between different species was analyzed by using the method of bioinformatics. By analyzing the interaction site between the hypoglycemic drug Miglitol and α-glucosidase of Beta vulgaris, and the characteristics of corresponding amino acid in other close genetic species, we found that Miglitol was located in a narrow binding pocket which recesses inside to the enzyme molecule. The interactions between them are mainly electrostatic interactions, hydrogen bonds and van der Waals forces. There are multiple O-H hydrogen bonds between drug and the enzyme molecules, which makes Miglitol a better inhibition because of the characteristics of strong water-solubility and polyhydroxy of the Miglitol. Through TMHMM prediction of the Beta vulgarisα-glucosidase sequence, it was found that there is no transmembrane region. The multiple sequence alignment suggested that 81.82% of the amino acids located in the interactive sites between Miglitol and Beta vulgarisα-glucosidase were conservative among the closest genetic species Camellia sinensis, Cucumis sativus, Gossypium arboretum, Spontaneum andMedicago truncatula. Among the conserved amino acids, the polar ones, such as Asp and Trp, were the most. This bioinformatics-based analysis can provide important scientific basis for further behavioral research of the hypoglycemic drugs in other species.
Key words:  α-glucosidase  Interaction  Sequence alignment  Phylogenetic relationships

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