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1篇 您的检索式：作者名="Meitong Huo"

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		题名	作者	年代	出处	被引量
	1	Lysine acetylation decreases enzyme activity and protein level of Escherichia coli lactate dehydrogenase显示文摘Lactate is an important bulk chemical with widespread applications and a major byproduct of other chemicals bioprocess in microbial fermentation.Lactate dehydrogenase A(LdhA)catalyzes the synthesis of lactate from pyruvate.Lysine acetylation is an evolutionarily conserved post-translational modification;however,the mech-anisms underlying the regulation of LdhA function by lysine acetylation in Escherichia coli remain poorly under-stood.Herein,we demonstrate acetylation of E.coli LdhA occurs via enzymatic and non-enzymatic mechanisms.Further,we show carbon source type and concentration affect the lysine acetylation status of LdhA via a non-enzymatic mechanism.Lysine acetylation significantly inhibits the enzymatic activity and protein level of LdhA.The results of the present study demonstrate lysine acetylation of E.coli LdhA is irreversible.Understanding of the effects of lysine acetylation on LdhA function may provide a new perspective for regulating lactate production in microbial synthesis.	Min Liu Meitong Huo Likun Guo Yingxin Fu Mo Xian Qingsheng Qi Wei Liu Guang Zhao	2022	Engineering Microbiology2022，2，4：	0

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