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Vitamin K epoxide reductases (VKORs) are a large family of integral membrane enzymes found from bacteria to humans. Human VKOR, specific target of warfarin, has both the epoxide and quinone reductase activity to maintain the vitamin K cycle. Bacterial VKOR homologs, however, are insensitive to warfarin inhibition and are quinone reductases incapable of epoxide reduction. What affords the epoxide reductase activity in human VKOR remains unknown. Here, we show that a representative bacterial VKOR homolog can be converted to an epoxide reductase that is also inhibitable by warfarin. To generate this new activity, we first substituted several regions surrounding the active site of bacterial VKOR by those from human VKOR based on comparison of their crystal structures. Subsequent systematic substitutions narrowed down to merely eight residues, with the addition of a membrane anchor domain, that are responsible for the epoxide reductase activity. Substitutions corresponding to N80 and Y139 in human VKOR provide strong hydrogen bonding interactions to facilitate the epoxide reduction. The rest of six substitutions increase the size and change the shape of the substrate‐binding pocket, and the membrane anchor domain stabilizes this pocket while allowing certain flexibility for optimal binding of the epoxide substrate. Overall, our study reveals the structural features of the epoxide reductase activity carried out by a subset of VKOR family in the membrane environment. [ABSTRACT FROM AUTHOR]

A novel fluorescent covalent organic framework containing trimethyl silicon group (COF-TMS) was designed and prepared via the Povarov reaction to be used to detect fluorine ions, on account of the interaction between the silicon and the fluorine ions. Trimethyl silicon, as an electron-donating functional group, was replaced with hydrogen atom and the electronic state of the whole material changed. In this process, the change of COF-TMS structure resulted in the fluorescence color changing from red to blue obviously. Furthermore, the structure and optical property of COF-TMS did not change when there are anions such as H2PO4−, ClO4−, SO42−, CO32−, Cl−, Br−, I−, and NO3− in the solution. Notably, the crystallinity also became particularly high in this process, with perfectly regular hexagonal pore structures being clearly observed in the micron range. This work provides a new idea for the future study of COFs in the field of fluorescence through the combination of COFs structure and fluorescence color transformation. [ABSTRACT FROM AUTHOR]

Although many prokaryotes have glycolysis alternatives, it's considered as the only energy-generating glucose catabolic pathway in eukaryotes. Here, we managed to create a hybrid-glycolysis yeast. Subsequently, we identified an inositol pyrophosphatase encoded by OCA5 that could regulate glycolysis and respiration by adjusting 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP 7) levels. 5-InsP 7 levels could regulate the expression of genes involved in glycolysis and respiration, representing a global mechanism that could sense ATP levels and regulate central carbon metabolism. The hybrid-glycolysis yeast did not produce ethanol during growth under excess glucose and could produce 2.68 g/L free fatty acids, which is the highest reported production in shake flask of Saccharomyces cerevisiae. This study demonstrated the significance of hybrid-glycolysis yeast and determined Oca5 as an inositol pyrophosphatase controlling the balance between glycolysis and respiration, which may shed light on the role of inositol pyrophosphates in regulating eukaryotic metabolism. [Display omitted] • Hybrid of glycolysis with the phosphoketolase pathway made an efficient cell factory • Oca5, identified as an inositol pyrophosphatase, degrading 5-InsP 7 to InsP 6 • InsPs control gene expression involved in glycolysis and respiration to balance fluxes • The mechanism of Oca5 regulating glycolysis and respiration was elaborated Glycolysis is considered as the only energy-generating glucose catabolic pathway in eukaryotes. Qin et al. establish a hybrid-glycolysis yeast that disrupts the Embden-Meyerhof-Parnas glycolysis pathway and introduced components of the phosphoketolase pathway. They further identify Oca5 as an inositol pyrophosphatase controlling the balance between glycolysis and respiration activities. [ABSTRACT FROM AUTHOR]

[Display omitted] • The COF-Tr-BA was prepared for selective adsorption and Li-S battery. • COF-Tr-BA shows excellent selectivity for genistein isomer by chemical interaction. • The introduction of boric acid group helps to improve electrochemical performance. Functional triazine-based covalent organic frameworks (COFs) with boric acid units, COF-Tr-BA, are designed and synthesized via cycloaddition of imine-linked COFs, COF-Tr, with (4-ethynylphenyl) boronic acid. Owing to the chemical interaction between boric acid units and adjacent dihydroxyl groups, COF-Tr-BA is used as the adsorbent for the selective adsorption of genistein isomer 4′6,7-trihydroxyisoflavone, showing an excellent selectivity and great adsorption performance with 5.4 times adsorption capacity (67.5 mg g−1) as high as 4′5,7-trihydroxyisoflavone (12.5 mg g−1). Meanwhile, COF-Tr-BA as the sulfur host for lithium-sulfur (Li-S) battery also exhibits a better electrochemical property, giving an initial discharge capacity up to 1349 mA h g−1 and a substantial capacity of 627 mA h g−1 after 200 cycles at 0.5C. It is attributed to the sulfiphilic interaction between the introduced boric acid groups and polysulfides (PSs), as well as the lithiophilic interaction between N atoms from quinoline and triazine moieties on the backbone of COF-Tr-BA and lithium ions (Li+), thus alleviating the dissolution and reducing the shuttle effect of LiPSs. The boric acid functionalized material COF-Tr-BA with the dual-function for selective adsorption and Li-S battery proposed here lays a significant foundation for multifunctional COFs as a versatile platform in practical application. [ABSTRACT FROM AUTHOR]