ReviewSub-cellular biochemistry2021
Recent Progress in Structural Studies on the GT-C Superfamily of Protein Glycosyltransferases.
Review in Sub-cellular biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Structural Insights into the Glycosylphosphatidylinositol Mannosyltransferase I Complex fromJournal of fungi (Basel, Switzerland) · 2025Article
- Pmt4 recognizes two separate acceptor sites to O-mannosylate in the S/T-rich regions of substrate proteins.Nature communications · 2025Article
- Structural Insights into the Protein Mannosyltransferase from Mycobacterium tuberculosis reveal a WW-Domain-Like Protein Motif in Bacteria.Communications biology · 2025Article
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Structure and Function of the Glycosylphosphatidylinositol Transamidase, a Transmembrane Complex Catalyzing GPI Anchoring of Proteins.Sub-cellular biochemistry · 2024Review
- Preparation of a Klebsiella pneumoniae conjugate nanovaccine using glycol-engineered Escherichia coli.Microbial cell factories · 2023Article
- The Search for Cryptic L-Rhamnosyltransferases on theJournal of fungi (Basel, Switzerland) · 2022Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein glycosylation is an essential covalent modification involved in protein secretion, stability, binding, folding, and activity. One or more sugars may be O-, N-, S-, or C-linked to specific amino acids by glycosyltransferases, which catalyze the transfer of these sugars from a phosphate-containing carrier molecule. Most glycosyltransferases are members of the GT-A, GT-B, or GT-C structural superfamilies. GT-C enzymes are integral membrane proteins that utilize a phospho-isoprenoid carrier for sugar transfer. To-date, two families of GT-Cs involved in protein glycosylation have been structurally characterized: the family represented by PglB, AglB, and Stt3, which catalyzes oligosaccharide transfer to Asn, and the family represented by Pmt1 and Pmt2, which catalyzes mannose transfer to Thr or Ser. This chapter reviews progress made over recent years on the structure and function of these two GT-C families.
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