Terpenoids,known for their structural and functional diversity,are highly valued,especially in food,cosmetics,and cleaning products.Microbial biosynthesis has emerged as a sustainable and environmentally friendly appr...Terpenoids,known for their structural and functional diversity,are highly valued,especially in food,cosmetics,and cleaning products.Microbial biosynthesis has emerged as a sustainable and environmentally friendly approach for the production of terpenoids.However,the natural enzymes involved in the synthesis of terpenoids have problems such as low activity,poor specificity,and insufficient stability,which limit the biosynthesis efficiency.Enzyme engineering plays a pivotal role in the microbial synthesis of terpenoids.By modifying the structures and functions of key enzymes,researchers have significantly improved the catalytic activity,specificity,and stability of enzymes related to terpenoid synthesis,providing strong support for the sustainable production of terpenoids.This article reviews the strategies for the modification of key enzymes in microbial synthesis of terpenoids,including improving enzyme activity and stability,changing specificity,and promoting mass transfer through multi-enzyme collaboration.Additionally,this article looks forward to the challenges and development directions of enzyme engineering in the microbial synthesis of terpenoids.展开更多
O-Mannosylation plays a vital role in the regulation of a variety range of biological processes,for instance,brain and muscle development.However,the precise function remains largely unknown due to its innate heteroge...O-Mannosylation plays a vital role in the regulation of a variety range of biological processes,for instance,brain and muscle development.However,the precise function remains largely unknown due to its innate heterogeneity.In this regard,it is still welcome to develop efficient methods to access diverse structurally-defined glycopeptides.In this study,a diversity-oriented assembly of O-mannosylα-dystroglycan(α-DG)glycopeptides has been achieved via a chemoenzymatic strategy.This strategy features(i)gram scale divergent synthesis of core m1,core m2 and core m3 mannosylated amino acids from judiciously designed protecting group strategies and chemical glycosidation;(i)efficient glycopeptide assembly via the optimized microwave-assisted solid phase peptide synthesis(SPpS);and(ii)enzymatic elaboration of the core glycan structures to install galactosyl and sialyl-galactosyl moieties.The efficiency and flexibility of this chemoenzymatic approach was demonstrated with the construction of 12 glycopeptides with different core m1,core m2 and core m3 mannosyl glycans,including a core m2 glycopeptide bearing a heptasaccharide for the first time.展开更多
文摘Terpenoids,known for their structural and functional diversity,are highly valued,especially in food,cosmetics,and cleaning products.Microbial biosynthesis has emerged as a sustainable and environmentally friendly approach for the production of terpenoids.However,the natural enzymes involved in the synthesis of terpenoids have problems such as low activity,poor specificity,and insufficient stability,which limit the biosynthesis efficiency.Enzyme engineering plays a pivotal role in the microbial synthesis of terpenoids.By modifying the structures and functions of key enzymes,researchers have significantly improved the catalytic activity,specificity,and stability of enzymes related to terpenoid synthesis,providing strong support for the sustainable production of terpenoids.This article reviews the strategies for the modification of key enzymes in microbial synthesis of terpenoids,including improving enzyme activity and stability,changing specificity,and promoting mass transfer through multi-enzyme collaboration.Additionally,this article looks forward to the challenges and development directions of enzyme engineering in the microbial synthesis of terpenoids.
基金This work is financially supported by the National Natural Science Foundation of China(Grant Nos.22177061,92053110,21977063,21907056)the China Postdoctoral Science Foundation(2020M680090)+2 种基金the Shenzhen Science and Technology Program(RCBS20200714114957255)the Open Projects Fund of Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology(2021CCG01&02)the Central Government Guide Local Science and Technology Development Funds(YDZX20203700002579).
文摘O-Mannosylation plays a vital role in the regulation of a variety range of biological processes,for instance,brain and muscle development.However,the precise function remains largely unknown due to its innate heterogeneity.In this regard,it is still welcome to develop efficient methods to access diverse structurally-defined glycopeptides.In this study,a diversity-oriented assembly of O-mannosylα-dystroglycan(α-DG)glycopeptides has been achieved via a chemoenzymatic strategy.This strategy features(i)gram scale divergent synthesis of core m1,core m2 and core m3 mannosylated amino acids from judiciously designed protecting group strategies and chemical glycosidation;(i)efficient glycopeptide assembly via the optimized microwave-assisted solid phase peptide synthesis(SPpS);and(ii)enzymatic elaboration of the core glycan structures to install galactosyl and sialyl-galactosyl moieties.The efficiency and flexibility of this chemoenzymatic approach was demonstrated with the construction of 12 glycopeptides with different core m1,core m2 and core m3 mannosyl glycans,including a core m2 glycopeptide bearing a heptasaccharide for the first time.
