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Tytuł:
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Discovery and mechanism of intestinal bacteria in enzymatic cleavage of C-C glycosidic bonds.
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Autorzy:
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Wei B; Key Laboratory of Marine Ecosystem and Biogeochemistry, State Oceanic Administration & Second Institute of Oceanography, Ministry of Natural Resources, 310012, Hangzhou, People's Republic of China.; College of Pharmaceutical Science & Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, Zhejiang University of Technology, 310014, Hangzhou, People's Republic of China.
Wang YK; College of Pharmaceutical Science & Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, Zhejiang University of Technology, 310014, Hangzhou, People's Republic of China.
Qiu WH; College of Pharmaceutical Science & Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, Zhejiang University of Technology, 310014, Hangzhou, People's Republic of China.
Wang SJ; College of Pharmaceutical Science & Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, Zhejiang University of Technology, 310014, Hangzhou, People's Republic of China.; Center for Human Nutrition, David Geffen School of Medicine, University of California, Rehabilitation Building 32-21, 1000 Veteran Avenue, Los Angeles, CA, 90024, USA.
Wu YH; Key Laboratory of Marine Ecosystem and Biogeochemistry, State Oceanic Administration & Second Institute of Oceanography, Ministry of Natural Resources, 310012, Hangzhou, People's Republic of China.
Xu XW; Key Laboratory of Marine Ecosystem and Biogeochemistry, State Oceanic Administration & Second Institute of Oceanography, Ministry of Natural Resources, 310012, Hangzhou, People's Republic of China. .
Wang H; College of Pharmaceutical Science & Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, Zhejiang University of Technology, 310014, Hangzhou, People's Republic of China. .
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Źródło:
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Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2020 Mar; Vol. 104 (5), pp. 1883-1890. Date of Electronic Publication: 2020 Jan 13.
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Typ publikacji:
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Journal Article; Review
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Język:
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English
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Imprint Name(s):
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Original Publication: Berlin ; New York : Springer International, c1984-
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MeSH Terms:
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Bacteria/*enzymology
Bacteria/*metabolism
Bacterial Proteins/*metabolism
Glycoside Hydrolases/*metabolism
Glycosides/*metabolism
Intestines/*microbiology
Animals ; Bacteria/isolation & purification ; Bacterial Proteins/genetics ; Biotransformation ; Glycoside Hydrolases/genetics ; Glycosides/chemistry ; Glycosylation ; Humans ; Molecular Structure
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Grant Information:
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2017YFE0103100 National Key Research and Development Program of China; 81773628 National Natural Science Foundation of China; 81741165 National Natural Science Foundation of China; No. D17012 National 111 Project
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Contributed Indexing:
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Keywords: C-glycosides; C–C glycosidic bond; Deglycosylation; Intestinal bacteria; Puerarin
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Substance Nomenclature:
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0 (Bacterial Proteins)
0 (C-glycoside)
0 (Glycosides)
EC 3.2.1.- (Glycoside Hydrolases)
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Entry Date(s):
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Date Created: 20200115 Date Completed: 20200219 Latest Revision: 20200219
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Update Code:
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20240105
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DOI:
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10.1007/s00253-019-10333-z
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PMID:
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31932892
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C-Glycosides, a special type of glycoside, are frequently distributed in many kinds of medicinal plants, such as puerarin and mangiferin, showing various and significant bioactivities. C-Glycosides are usually characterized by the C-C bond that forms between the anomeric carbon of sugar moieties and the carbon atom of aglycon, which is usually resistant against acidic hydrolysis and enzymatic treatments. Interestingly, C-glycosides could be cleaved by several intestinal bacteria, but whether the enzymatic cleavage of C-C glycosidic bond is reduction or hydrolysis has been controversial; furthermore, whether existence of a "C-glycosidase" directly catalyzing the cleavage is not clear. Here we review research advances about the discovery and mechanism of intestinal bacteria in enzymatic cleavage of C-C glycosidic bond with an emphasis on the identification of enzymes manipulation the deglycosylation. Finally, we give a brief conclusion about the mechanism of C-glycoside deglycosylation and perspectives for future study in this field.
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