1. Fructuronate-tagaturonate epimerase UxaE from Cohnella laeviribosi has a versatile TIM-barrel scaffold suitable for a sugar metabolizing biocatalyst
- Author
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Kyung-Chul Shin, Dae Wook Kim, Hyunjae Park, Moon Young Choi, Diem Quynh Nguyen, Yoon Sik Park, Lin-Woo Kang, Thien-Hoang Ho, and Deok-Kun Oh
- Subjects
animal structures ,food.ingredient ,Pectin ,Carbohydrates ,Racemases and Epimerases ,02 engineering and technology ,Biochemistry ,Catalysis ,Cofactor ,Phosphates ,Substrate Specificity ,Cell wall ,03 medical and health sciences ,food ,Structural Biology ,Catalytic Domain ,TIM barrel ,Molecular Biology ,030304 developmental biology ,Bacillales ,0303 health sciences ,biology ,Chemistry ,food and beverages ,Active site ,General Medicine ,021001 nanoscience & nanotechnology ,Combinatorial chemistry ,Xylan ,carbohydrates (lipids) ,Metals ,Biocatalysis ,biology.protein ,Pectins ,Xylans ,Sugars ,0210 nano-technology - Abstract
Xylan and pectin are major structural components of plant cell walls. There are two independent catabolic pathways for xylan and pectin. UxaE bridges these two pathways by reversibly epimerizing D-fructuronate and D-tagaturonate. The crystal structure of UxaE from Cohnella laeviribosi (ClUxaE) shows a core scaffold of TIM-barrel with a position-changing divalent metal cofactor. ClUxaE has the flexible metal-coordination loop to allow the metal shift and the extra domains to bind a phosphate ion in the active site, which are important for catalysis and substrate specificity. Elucidation of the structure and mechanism of ClUxaE will assist in understanding the catalytic mechanism of UxaE family members, which are useful for processing both xylan and pectin-derived carbohydrates for practical and industrial purposes, including the transformation of agricultural wastes into numerous valuable products.
- Published
- 2020
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