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β4-Galactosyltransferase-I

  • Nancy L. Shaper
  • Joel H. Shaper

Abstract

The enzyme β4-galactosyltransferase-I (β4GalT-I; UDP-Gal:GlcNAc β4-galactosyltransferase; EC 2.4.1.38) is a constitutively expressed, trans-Golgi resident, type II membrane-bound glycoprotein that is widely distributed in vertebrates. The protein domain structure established for β4GalT-I consists of: (1) a short NH2-terminal cytoplasmic domain of 11 or 24 amino acids depending on the protein isoform (Shaper et al. 1988; Russo et al. 1990); (2) a large COOH-terminal luminal domain containing the catalytic center (~270 amino acids) linked to a single transmembrane domain (19 amino acids) through a glycosylated peptide segment (~86 amino acids) termed the stem region. In essentially all vertebrate tissues, the primary function of β4GalT-I is to catalyze the transfer of Gal from UDP-Gal to GlcNAcβ-R, forming the N-acetyllactosamine (Galβ1-4GlcNAcβ1-R) or poly-N-acetyllactosamine structures assembled on glycoconjugates.

Keywords

Mammary Gland Round Spermatid Stem Region Acceptor Substrate Golgi Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Nancy L. Shaper
    • 1
  • Joel H. Shaper
    • 1
    • 2
  1. 1.Cell Structure and Function Laboratory, Johns Hopkins Oncology Center CRB-345The Johns Hopkins University School of MedicineBaltimoreUSA
  2. 2.Department of Pharmacology and Molecular SciencesThe Johns Hopkins University School of MedicineBaltimoreUSA

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