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Article

Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation.

Nature communications - 4 Dec 2020

Klontz Erik H, Li Chao, Kihn Kyle, Fields James K, Beckett Dorothy, Snyder Greg A, Wintrode Patrick L, Deredge Daniel, Wang Lai-Xi, Sundberg Eric J

Abstract excerpt

Fucosylation is important for the function of many proteins with biotechnical and medical applications. Alpha-fucosidases comprise a large enzyme family that recognizes fucosylated substrates with diverse α-linkages on these proteins. Lactobacillus casei produces an α-fucosidase, called AlfC, with specificity towards α(1,6)-fucose, the only linkage found in human N-glycan core fucosylation. AlfC and certain point...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 33277506
DOI: 10.1038/s41467-020-20044-z
PMCID: PMC7718225

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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