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- W2238819076 abstract "Abstract Most enzymes that act on carbohydrates include non-catalytic carbohydrate-binding modules (CBMs) that recognize and target carbohydrates. CBMs bring their appended catalytic modules into close proximity with the target substrate and increase the hydrolytic rate of enzymes acting on insoluble substrates. We previously identified a novel CBM (CBM C5614-1 ) at the C-terminus of endoglucanase C5614-1 from an uncultured microorganism present in buffalo rumen. In the present study, that the functional region of CBM C5614-1 involved in ligand binding was localized to 134 amino acids. Two representative homologs of CBM C5614-1 , sharing the same ligand binding profile, targeted a range of β-linked polysaccharides that adopt very different conformations. Targeted substrates included soluble and insoluble cellulose, β-1,3/1,4-mixed linked glucans, xylan and mannan. Mutagenesis revealed that three conserved aromatic residues (Trp-380, Tyr-411 and Trp-423) play an important role in ligand recognition and targeting. These results suggest that CBM C5614-1 and its homologs form a novel CBM family (CBM72) with a broad ligand-binding specificity. CBM72 members can provide new insight into CBM-ligand interactions and may have potential in protein engineering and biocatalysis." @default.
- W2238819076 created "2016-06-24" @default.
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- W2238819076 date "2016-01-14" @default.
- W2238819076 modified "2023-09-23" @default.
- W2238819076 title "Identification of a novel family of carbohydrate-binding modules with broad ligand specificity" @default.
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- W2238819076 doi "https://doi.org/10.1038/srep19392" @default.
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