Effects Of Protein Acylation On Metabolisms Of Acetate And Propionate

Protein lysine acylation is an important mechanism that occurs in cells of all domains of life and has emerged as a critical modification for the control of many aspects of cellular physiology.There are two acylation modalities in the living body:enzymatic acylation based on acyltransferase and non-enzymatic acylation reaction one is enzymatic acylation,the other is non-enzymatic acylation.Studies have shown that protein lysine acylation plays an important role in responding to nutrient metabolism,regulating protein function and influencing activity of metabolic enzyme metabolites.In order to understand the difference between the two kinds of protein acylation modification and the its effect ton acetate and piopionate metabolism,our research contents are as follows:?1?Study on the acetate metabolism and the comparative difference between two acylation?nonenzymatic catalysis and enzymatic catalysis?mechanisms.Acs A?Acetyl-CoA Synthase,EC:6.2.1.1?is a key enzyme for acetate metabolism.Studies have shown that the activity of AcsA is regulated by acylation modification.In this paper,two acylation mechanisms of AcsA were studied,and we described the post-translational modification system,found that the acylation modification was time-and concentration-dependent,elucidated the specificity and dynamic change of the acylation sites,revealed the differences and linkages of the different acylation mechanisms,extended our understanding of the acylation modification mechanism and afforded foundation and some fresh interference nodes of the subsequent transformation of the strain based on the acylation modification.?2?Effects of acylation of propionyl-CoA synthetase?PrpE?on erythromycin production in Saccharopolyspora erythraea.Propionyl-CoA?Pr-CoA?is an important acylated donor and is also a precursor of erythromycin synthesis in Saccharopolyspora erythraea.This study was conducted from the transcription level and the post-translational modification of the key enzyme PrpE induced by propionate.We found that the propionylation can regulate the propionyl-CoA synthetase?EC:6.2.1.17,PrpE?,and we also modified the strain in the acylation layer by overexpressing SACE₁780 with 140%production improvement relative to WB of erythromycin.This study not only improved the protein lysine acylation of actinomycetes,but also established a strategy for the intervention of production of erythromycin by acylation modification.