Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis

doi:10.3389/fbioe.2022.966062

CORC > 海洋研究所 > 中国科学院海洋研究所

	Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis
	Liu, Min 3; Huo, Meitong 3; Liu, Changshui 2; Guo, Likun 3; Ding, Yamei 2; Ma, Qingjun 2; Qi, Qingsheng 3; Xian, Mo 1; Zhao, Guang 1,3
刊名	FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
	2022-08-16
卷号	10 页码:12
关键词	lysine acetylation lactate dehydrogenase A enzyme activity metabolic engineering lactate synthesis
ISSN号	2296-4185
DOI	10.3389/fbioe.2022.966062
通讯作者	Xian, Mo(xianmo@qibebt.ac.cn) ; Zhao, Guang(zhaoguang@sdu.edu.cn)
英文摘要	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.
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
语种	英语
出版者	FRONTIERS MEDIA SA
WOS记录号	WOS:000848354100001
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/180867]
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.Qingdao Inst Bioenergy & Bioproc Technol, Chinese Acad Sci, CAS Key Lab Biobased Mat, Qingdao, Peoples R China 2.Chinese Acad Sci, Inst Oceanol, Qingdao, Peoples R China 3.Shandong Univ, State Key Lab Microbial Technol, 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.