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Literature DB >> 7358666

Substrate specificities of rat liver microsomal glucosidases which process glycoproteins.

Abstract

The substrate specificities of rat liver microsomal glucosidases I and II, which hydrolyze oligosaccharides of the composition Glc3-1Man9GlcNAc, were investigated. Glucosidases I and II were shown to have a specific and necessary interaction with the 6'-pentamannosyl branch of their oligosaccharide substrates; activity was reduced when mannose residues were removed from this branch. Both glucosidases responded to features at the reducing end of the oligosaccharide substrates; activity was lower towards lipid-linked and peptide-linked substrates than towards free oligosaccharide substrates. In addition, the glucosidases appeared to discriminate between oligosaccharides linked to lipid and oligosaccharides linked to peptide. We conclude that rat liver microsomal glucosidases I and II interact with extensive portions of oligosaccharide structure in addition to the glucose residues which they hydrolyze.

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Year: 1980 PMID： 7358666

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

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Cited

30 in total

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Journal: J Biol Chem Date: 2008-02-26 Impact factor: 5.157

2. Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.

Authors: Linda J Olson; Ramiro Orsi; Francis C Peterson; Armando J Parodi; Jung-Ja P Kim; Cecilia D'Alessio; Nancy M Dahms
Journal: Biochemistry Date: 2015-06-24 Impact factor: 3.162

3. Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum.

Authors: Linda J Olson; Ramiro Orsi; Solana G Alculumbre; Francis C Peterson; Ivan D Stigliano; Armando J Parodi; Cecilia D'Alessio; Nancy M Dahms
Journal: J Biol Chem Date: 2013-04-22 Impact factor: 5.157

4. Golgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control.

Authors: C Zuber; M J Spiro; B Guhl; R G Spiro; J Roth
Journal: Mol Biol Cell Date: 2000-12 Impact factor: 4.138

5. Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.

Authors: Tadashi Satoh; Takayasu Toshimori; Masanori Noda; Susumu Uchiyama; Koichi Kato
Journal: Protein Sci Date: 2016-09-14 Impact factor: 6.725

6. Synthesis of fluorine substituted oligosaccharide analogues of monoglucosylated glycan chain, a proposed ligand of lectin-chaperone calreticulin and calnexin.

Authors: Yukishige Ito; Shinya Hagihara; Midori A Arai; Ichiro Matsuo; Maki Takatani
Journal: Glycoconj J Date: 2004 Impact factor: 2.916

Substrate specificities of rat liver microsomal glucosidases which process glycoproteins.

Review 1. Getting in and out from calnexin/calreticulin cycles.

2. Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.

3. Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum.

4. Golgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control.

5. Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.

6. Synthesis of fluorine substituted oligosaccharide analogues of monoglucosylated glycan chain, a proposed ligand of lectin-chaperone calreticulin and calnexin.

7. Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

8. Alterations in the structure of the oligosaccharide of vesicular stomatitis virus G protein by swainsonine.

9. Effect of castanospermine on the structure and secretion of glycoprotein enzymes in Aspergillus fumigatus.

10. NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation.