2. Academic Validation
  3. Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15

Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15

  • FEBS Lett. 2004 May 21;566(1-3):17-24. doi: 10.1016/j.febslet.2004.03.108.
Lamei Cheng 1,  Kouichi Tachibana,  Hiroko Iwasaki,  Akihiko Kameyama,  Yan Zhang,  Tomomi Kubota,  Toru Hiruma,  Kahori Tachibana,  Takashi Kudo,  Jian-Ming Guo,  Hisashi Narimatsu
Affiliations

Affiliation

  • 1 Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan.
PMID: 15147861 DOI: 10.1016/j.febslet.2004.03.108
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.

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