Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Catalysis
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Glycosylation
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Humans
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Isoenzymes
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Molecular Sequence Data
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N-Acetylgalactosaminyltransferases / genetics*
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N-Acetylgalactosaminyltransferases / metabolism*
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Oligopeptides / chemistry
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Oligopeptides / metabolism
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Polypeptide N-acetylgalactosaminyltransferase
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Alignment
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
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Substrate Specificity
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Tissue Distribution
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Transcription, Genetic
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Uridine Diphosphate N-Acetylgalactosamine / metabolism
Substances
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Isoenzymes
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Oligopeptides
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Recombinant Proteins
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Uridine Diphosphate N-Acetylgalactosamine
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N-Acetylgalactosaminyltransferases
Associated data
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GENBANK/AB078149
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GENBANK/BG699346
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GENBANK/BG714178
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GENBANK/BG715977