Structure, Function and Mechanism of N‐Glycan Processing Enzymes: endo ‐α‐1,2‐Mannanase and endo ‐α‐1,2‐Mannosidase

Abstract: While most glycosidases that act on N‐linked glycans remove a single sugar residue at a time, endo‐α‐1,2‐mannosidases and endo‐α‐1,2‐mannanases of glycoside hydrolase family GH99 cut within a chain and remove two or more sugar residues. They are stereochemically retaining enzymes that use an enzymatic mechanism involving an epoxide intermediate. Human endo‐α‐1,2‐mannosidase (MANEA) trims glucosylated mannose residues; the endomannosidase pathway provides a glucosidase‐independent pathway for glycoprotein maturation. Cell‐active MANEA inhibitors alter N‐glycan processing and reduce infectivity of dengue virus, demonstrating that MANEA has potential as a host‐directed antiviral target. Sequence‐related enzymes from gut Bacteroides spp. exhibit endo‐α‐1,2‐mannosidase activity and are a fruitful test bed for structure‐guided inhibitor development. The genes encoding the Bacteroides spp. enzymes sit within polysaccharide utilization loci and are preferential endo‐α‐1,2‐mannanases.

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch

References and Relationships

• Bibliographic citation: Structure, Function and Mechanism of N‐Glycan Processing Enzymes: endo ‐α‐1,2‐Mannanase and endo ‐α‐1,2‐Mannosidase ; day:19 ; month:10 ; year:2022 ; extent:1 ; Israel journal of chemistry ; (19.10.2022) (gesamt 1)

Contributors, Places and Time

• Creator: Burchill, Laura ; Males, Alexandra ; Kaur, Arashdeep ; Davies, Gideon ; Williams, Spencer J.

Further information

• DOI: 10.1002/ijch.202200067
• URN: urn:nbn:de:101:1-2022102015133727935742
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 15.08.2025, 7:25 AM CEST