| RRC ID |
58962
|
| 著者 |
Miura K, Hakamata W, Tanaka A, Hirano T, Nishio T.
|
| タイトル |
Discovery of human Golgi β-galactosidase with no identified glycosidase using a QMC substrate design platform for exo-glycosidase.
|
| ジャーナル |
Bioorg Med Chem
|
| Abstract |
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.
|
| 巻・号 |
24(6)
|
| ページ |
1369-75
|
| 公開日 |
2016-3-15
|
| DOI |
10.1016/j.bmc.2016.02.010
|
| PII |
S0968-0896(16)30090-6
|
| PMID |
26875935
|
| MeSH |
Cell Line, Tumor
Fluorescence
Glycoside Hydrolases / chemistry
Glycoside Hydrolases / metabolism*
Golgi Apparatus / enzymology*
HeLa Cells
Humans
Indolequinones / chemistry
Indolequinones / metabolism*
Molecular Structure
beta-Galactosidase / chemistry*
beta-Galactosidase / metabolism*
|
| IF |
3.073
|
| 引用数 |
3
|
| リソース情報 |
| ヒト・動物細胞 |
HeLa(RCB0007)
SK-N-SH(RCB0426) |
