Discovery of human Golgi β-galactosidase with no identified glycosidase using a QMC substrate design platform for exo-glycosidase

Kazuki Miura, Wataru Hakamata, Ayako Tanaka, Takako Hirano, Toshiyuki Nishio

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Post-translational modifications (PTMs) of proteins play important roles in the physiology of eukaryotes. In the PTMs, non-reversible glycosylations are classified as N-glycosylations and O-glycosylations, and are catalyzed by various glycosidases and glycosyltransferases. However, β-glycosidases are not known to play a role in N- and O-glycan processing, although both glycans provide partial structures as substrates for β-galactosidase and β-N-acetylglucosaminidase in the Golgi apparatus of human cells. We explored human Golgi β-galactosidase using fluorescent substrates based on a quinone methide cleavage (QMC) substrate design platform that was previously developed to image exo-type glycosidases in living cells. As a result, we discovered a novel Golgi β-galactosidase in human cells. It is possible to predict a novel and important function in glycan processing of this β-galactosidase, because various β-galactosyl linkages in N- and O-glycans exist in Golgi apparatus. In addition, these results show that the QMC platform is excellent for imaging exo-type glycosidases.

Original languageEnglish
Pages (from-to)1369-1375
Number of pages7
JournalBioorganic and Medicinal Chemistry
Issue number6
Publication statusPublished - 2016 Mar 15
Externally publishedYes


  • Fluorescent imaging
  • Glycan processing
  • Golgi apparatus
  • Post-translational modifications
  • Quinone methide cleavage
  • β-Galactosidase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry


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