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- W4387142893 abstract "Sulfated fucans are important marine polysaccharides with various bioactivities. Fucanases are desirable tools for the structural elucidations and oligosaccharides preparation of sulfated fucans. Herein, a gene with unknown function was screened from a sulfated fucan utilization locus in genome of marine bacterium Wenyingzhuangia aestuarii OF219 with the assistance of a machine learning approach on the structural biology. An undefined catalytic domain that presented in this gene was further cloned and expressed in Escherichia coli. Utilizing a sulfated fucan tetrasaccharide with definite structure as substrate, the endo-acting cleavage point of expressed protein (named FunxxxA) was identified as the α-l-1,3-glycosidic bond between Fucp and Fucp(2OSO3−). FunxxxA demonstrated a novel cleavage specificity, that is the subsite −1 could tolerate α-l-Fucp, and the subsite +1 could tolerate α-l-Fucp(2OSO3−). A homologue of FunxxxA was also validated to display the endo-1,3-fucanse activity. The sequence novelty of FunxxxA and its homologue defines a new glycoside hydrolase family." @default.
- W4387142893 created "2023-09-29" @default.
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- W4387142893 date "2023-09-01" @default.
- W4387142893 modified "2023-09-29" @default.
- W4387142893 title "Discovery of a catalytic domain defines a new glycoside hydrolase family containing endo-1,3-fucanase" @default.
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- W4387142893 doi "https://doi.org/10.1016/j.carbpol.2023.121442" @default.
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