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Comparative Study
. 2004 May 21;566(1-3):17-24.
doi: 10.1016/j.febslet.2004.03.108.

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

Lamei Cheng  1 , Kouichi Tachibana, Hiroko Iwasaki, Akihiko Kameyama, Yan Zhang, Tomomi Kubota, Toru Hiruma, Kahori Tachibana, Takashi Kudo, Jian-Ming Guo, Hisashi Narimatsu
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Free article
Comparative Study

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

Lamei Cheng et al. FEBS Lett. .
Free article

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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