Publication | Open Access
Characterization of a novel human UDP‐GalNAc transferase, pp‐GalNAc‐T15
69
Citations
37
References
2004
Year
Human Udp‐galnacBiosynthesisBioorganic ChemistryBiochemistryMolecular Biological MethodNatural SciencesBioanalysisGlycobiologyBiochemical GeneticsMolecular BiologyPeptide SynthesisPeptide ScienceCatalytic ActivityUnique Catalytic ActivityChemical BiologyMedicineProtein BiosynthesisGlycosylation
We have cloned, expressed and characterized a novel member of the human UDP‐GalNAc:polypeptide N ‐acetylgalactosaminyltransferase (pp‐GalNAc‐T) family, pp‐GalNAc‐T15. The pp‐GalNAc‐T15 transcript was ubiquitously expressed in human tissues. Recombinant pp‐GalNAc‐T15 transferred N ‐acetylgalactosamine (GalNAc) toward a panel of mucin‐derived peptide substrates in vitro. Although pp‐GalNAc‐T15 showed significantly less catalytic activity than pp‐GalNAc‐T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp‐GalNAc‐T15 is a novel member of the human pp‐GalNAc‐T family with unique catalytic activity.
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