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作 者:左青青 钱露 闻伟锷 徐德林 刘朝波 钱刚 李林 Zuo Qingqing;Qian Lu;Wen Wei’e;Xu Delin;Liu Chaobo;Qian Gang;Li Lin(Department of Cell Biology,Zunyi Medical University,Zunyi Guizhou 563099,China;The First Clinical Institute,Zunyi Medical University,Zunyi Guizhou 563099,China)
机构地区:[1]遵义医科大学细胞生物学教研室,贵州遵义563099 [2]遵义医科大学第一临床学院,贵州遵义563099
出 处:《遵义医科大学学报》2021年第1期42-47,共6页Journal of Zunyi Medical University
基 金:国家自然科学基金资助项目(NO:31560079,31560087);遵义医科大学精英人才工程项目。
摘 要:目的分析千里光过氧化氢酶序列结构,对其功能进行预测。方法采用ORF、ExpasyProt等多种生物信息学软件对千里光转录组数据库挑选出的过氧化氢酶核苷酸序列,编码蛋白质的性质和功能进行分析。结果千里光过氧化氢酶核酸序列全长1521 bp,共编码506个氨基酸残基,无信号肽,是亲水性蛋白,预测存在磷酸化位点67个,糖基化位点156个。与33个近缘物种的过氧化氢酶基因blast比对发现,该酶在物种进化上有较高的保守性(相似度>96%),系统进化分析表明,千里光与向日葵、艾菊等4种菊科植物分属不同亚支,表明千里光CAT在进化上亲缘性远于其他4种菊科植物。结论千里光过氧化氢酶结构保守,存在较丰富的磷酸化与糖基化位点,在进化上与其他4种菊科植物亲缘性较远。Objective To study and predict the structure and function of catalase(CAT)in Senecio scandens(S.scandens)Buch.-Ham.ex D.Don.Methods The nucleotide sequence of catalase was selected from S.scandens transcriptome database and the structure and properties with functions were further analyzed by several bioinformatics software as ORF,ExpasyProt and so on.Results The length of S.scandens cat gene was 1521 bp,encoding 506 amino acids,documented as a hydrophilic protein without signal peptide,and obtained with 67 phosphorylation sites and 156 glycosylation sites.Blasted with other cat genes showed this enzyme had high homology in 33 species and the similarity was more than 96%.The phylogenetic character showed cat in S.scandens with cat in 4 species of Compositae plants,such as sunflower and mugwort belong to 2 subfamily,indicating rather distant phylogenetic relationships with four Compositae members.Conclusion The sequence of cat in S.scandens presents with conserved structure and rather abundant phosphorylation sites and glycosylation sites and is much distant to the other compositae in evolution.
分 类 号:R114[医药卫生—卫生毒理学]
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