植物乳杆菌LY-78乳酸脱氢酶基因的生物信息学分析

发布时间：2018-05-23 12:10

本文选题：植物乳杆菌 + 乳酸脱氢酶　；参考：《食品科学》2017年08期

【摘要】：目的:探究植物乳杆菌LY-78菌株全部5个乳酸脱氢酶基因及其编码蛋白质的结构和功能。方法:应用多种生物信息学软件对植物乳杆菌LY-78菌株的5个乳酸脱氢酶基因及氨基酸序列进行结构分析和功能预测。结果:植物乳杆菌LY-78中5个乳酸脱氢酶的核苷酸及氨基酸序列均具有较高的保守性,均为位于细胞质的热稳定性、非分泌、非跨膜蛋白,除了ldh L3基因,其余4个基因均具有各自高度保守的功能位点和结构域,均存在典型的烟酰胺腺嘌呤二核苷酸(nicotinamide adenine dinucleotide,NAD~+)结合位点序列GXGXXG。结论:乳酸脱氢酶D1(D1-lactate dehydrogenase,D1-LDH)、D2-LDH、L1-LDH及L2-LDH均具有完整的功能位点和结构域,很可能具有真正的乳酸脱氢酶活性,L3-LDH由于缺失NAD~+结合结构域和功能位点,因而可能不具有乳酸脱氢酶活性,这些分析结果为今后植物乳杆菌乳酸脱氢酶基因改造和苯乳酸合成代谢机制研究提供了必要的理论基础。
[Abstract]:Aim: to investigate the structure and function of all 5 lactate dehydrogenase genes and their encoded proteins in Lactobacillus plantarum LY-78 strain. Methods: the structure and function of 5 lactate dehydrogenase genes and amino acid sequences of Lactobacillus plantarum LY-78 strains were analyzed and predicted by bioinformatics software. Results: the nucleotides and amino acid sequences of five lactate dehydrogenase in Lactobacillus plantarum LY-78 were all highly conserved, all of them were located in the cytoplasmic thermal stability, non-secretory, non-transmembrane protein, except for ldh L3 gene. The other four genes all had their own highly conserved functional sites and domains, and all had typical nicotinamide adenine dinucleotide- NAD- binding site GXGXXG. Conclusion: L1-LDH and L2-LDH have complete functional sites and domains. It is possible that L3-LDH has no lactate dehydrogenase activity due to the absence of NAD- binding domain and functional site. These results provide a theoretical basis for the further study of Lactobacillus plantarum lactate dehydrogenase gene transformation and the metabolic mechanism of phenyllactic acid biosynthesis.
【作者单位】：黑龙江八一农垦大学食品学院;国家杂粮工程技术研究中心;
【基金】：黑龙江八一农垦大学研究生创新科研项目(YJSCX2016-Y37) 黑龙江省青年科学基金项目(QC2014C020)
【分类号】：TS201.3

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