Description: The GlycoEnzDB is a manually curated glycoEnzyme database, primarily focused on humans. It covers 390 enzymes across 28 pathway maps. Facilities are also available to create custom glycosylation reaction pathways using experimental data in SBML format and for pathway simulation
Contacts: Sriram Neelamegham (email@example.com), Yusen Zhou (firstname.lastname@example.org) or Ted Groth (email@example.com).
• MGAT3 or GnT-III transfers β1,4-linked GlcNAc to the α1,4-linked Man in N-glycans. The resulting structure is termed 'bisecting GlcNAc', and plays a regulatory role(s) in the biosynthesis of complex and hybrid N-glycans.
• Prior MGAT1 activity is necessary for MGAT3 action. Previous βGal addition inhibits future MGAT3 activity. Prior α(1-6)fucosylation does not affect MGAT3, but bisecting structures will hinder core-fucosylation.
• Addition of MGAT3 also terminates N-glycan branching by inhibiting other GlcNAcTs.
• Overexpression of MGAT3 prevents N-glycan branching, reduces metastatic potential, lowers galectin lattice formation and inhibits epithelia-mesenchymal transition (EMT) induced by TGF-β1.