IOCAS-IR
Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis
Liu, Min1; Huo, Meitong1; Liu, Changshui2; Guo, Likun1; Ding, Yamei2; Ma, Qingjun2; Qi, Qingsheng1; Xian, Mo3; Zhao, Guang1,3
2022-08-16
发表期刊FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
ISSN2296-4185
卷号10页码:12
通讯作者Xian, Mo(xianmo@qibebt.ac.cn) ; Zhao, Guang(zhaoguang@sdu.edu.cn)
摘要As an evolutionarily conserved posttranslational modification, protein lysine acetylation plays important roles in many physiological and metabolic processes. However, there are few reports about the applications of lysine acetylation in metabolic regulations. Lactate is a main byproduct in microbial fermentation, and itself also an important bulk chemical with considerable commercial values in many fields. Lactate dehydrogenase (LdhA) is the key enzyme catalyzing lactate synthesis from pyruvate. Here, we reported that Escherichia coli LdhA can be acetylated and the acetylated lysine sites were identified by mass spectrometry. The effects and regulatory mechanisms of acetylated sites on LdhA activity were characterized. Finally, lysine acetylation was successfully used to regulate the lactate synthesis. LdhA (K9R) mutant overexpressed strain improved the lactate titer and glucose conversion efficiency by 1.74 folds than that of wild-type LdhA overexpressed strain. LdhA (K154Q-K248Q) mutant can inhibit lactate accumulation and improve 3HP production. Our study established a paradigm for lysine acetylation in lactate synthesis regulation and suggested that lysine acetylation may be a promising strategy to improve the target production and conversion efficiency in microbial synthesis. The application of lysine acetylation in regulating lactate synthesis also provides a reference for the treatment of lactate-related diseases.
关键词lysine acetylation lactate dehydrogenase A enzyme activity metabolic engineering lactate synthesis
DOI10.3389/fbioe.2022.966062
收录类别SCI
语种英语
资助项目National Key Research and Development Program of China ; National Natural Science Foundation of China[2021YFC2100503] ; Young Scholars Program of Shandong University[32170085] ; Young Scholars Program of Shandong University[31961133014] ; Distinguished Scholars Program of Shandong University ; Foundation for Innovative Research Groups of State Key Laboratory of Microbial Technology ; Fundamental Research Funds for the Central Universities
WOS研究方向Biotechnology & Applied Microbiology ; Science & Technology - Other Topics
WOS类目Biotechnology & Applied Microbiology ; Multidisciplinary Sciences
WOS记录号WOS:000848354100001
出版者FRONTIERS MEDIA SA
引用统计
被引频次:4[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.qdio.ac.cn/handle/337002/180868
专题中国科学院海洋研究所
通讯作者Xian, Mo; Zhao, Guang
作者单位1.Shandong Univ, State Key Lab Microbial Technol, Qingdao, Peoples R China
2.Chinese Acad Sci, Inst Oceanol, Qingdao, Peoples R China
3.Qingdao Inst Bioenergy & Bioproc Technol, Chinese Acad Sci, CAS Key Lab Biobased Mat, Qingdao, Peoples R China
推荐引用方式
GB/T 7714
Liu, Min,Huo, Meitong,Liu, Changshui,et al. Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis[J]. FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY,2022,10:12.
APA Liu, Min.,Huo, Meitong.,Liu, Changshui.,Guo, Likun.,Ding, Yamei.,...&Zhao, Guang.(2022).Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis.FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY,10,12.
MLA Liu, Min,et al."Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis".FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY 10(2022):12.
条目包含的文件
条目无相关文件。
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Liu, Min]的文章
[Huo, Meitong]的文章
[Liu, Changshui]的文章
百度学术
百度学术中相似的文章
[Liu, Min]的文章
[Huo, Meitong]的文章
[Liu, Changshui]的文章
必应学术
必应学术中相似的文章
[Liu, Min]的文章
[Huo, Meitong]的文章
[Liu, Changshui]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。