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| http://dx.doi.org/10.3389/fnut.2024.1427857 | DOI Listing |
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Characterization of a novel D-sorbitol dehydrogenase from Faunimonas pinastri A52C2.
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Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, China.
The enzyme D-sorbitol dehydrogenase (SLDH) facilitates the conversion of D-sorbitol to L-sorbose. While current knowledge of this enzyme class predominantly centers on Gluconobacter oxydans, the catalytic properties of enzymes from alternative sources, particularly their substrate specificity and coenzyme dependency, remain ambiguous. In this investigation, we conducted BLASTp analysis and screened out a novel SLDH (Fpsldh) from Faunimonas pinastri A52C2.
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Thioredoxin reductase 1 (TrxR1) is an important therapeutic target for nonsmall cell lung cancer (NSCLC) treatment due to its overexpression in NSCLC cells. In this work, to address the deficiency that sesquiterpene lactone containing α-methylene-γ-lactone moiety was rapidly metabolized by endogenous nucleophiles, series of novel thioether derivatives were designed and synthesized based on a reactive oxygen species (ROS)-triggered prodrug strategy. Among them, prodrug exhibited potent cytotoxicity against NSCLC cells and better release rates in response to ROS.
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Covering 1948 up to October 2024Sorbicillinoids are a growing class of natural products (NPs) that stem from a variety of fungi including members of the orders and . This compound class is unique in its combination of structural complexity and pharmaceutically relevant biological activities. The majority of the sorbicillinoids, which are named after the common hexaketide precursor sorbicillin, exhibit anti-inflammatory, antimicrobial, cytotoxic, phytotoxic, and other selective enzyme inhibitory activities.
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