Jack bean α-mannosidase digestion profile of hybrid-type N-glycans: effect of reaction pH on substrate preference.
Biochimie
; 93(4): 766-71, 2011 Apr.
Article
em En
| MEDLINE
| ID: mdl-21256916
ABSTRACT
Jack bean α-mannosidase (JBM) is a well-studied plant vacuolar α-mannosidase, and is widely used as a tool for the enzymatic analysis of sugar chains of glycoproteins. In this study, the JBM digestion profile of hybrid-type N-glycans was examined using pyridylamino (PA-) sugar chains. The digestion efficiencies of the PA-labeled hybrid-type N-glycans Manα1,6(Manα1,3)Manα1,6(GlcNAcß1,2Manα1,3)Manß1,4GlcNAcß1,4GlcNAc-PA (GNM5-PA) and Manα1,6(Manα1,3)Manα1,6(Galß1,4GlcNAcß1,2Manα1,3)Manß1,4GlcNAcß1,4GlcNAc-PA (GalGNM5-PA) were significantly lower than that of the oligomannose-type N-glycan Manα1,6(Manα1,3)Manα1,6Manß1,4GlcNAcß1,4GlcNAc-PA (M4-PA), and the trimming pathways of GNM5-PA and GalGNM5-PA were different from that of M4-PA, suggesting a steric hindrance to the JBM activity caused by GlcNAcß1-2Man(α) residues of the hybrid-type N-glycans. We also found that the substrate preference of JBM for the terminal Manα1-6Man(α) and Manα1-3Man(α) linkages in the hybrid-type N-glycans was altered by the change in reaction pH, suggesting a pH-dependent change in the enzyme-substrate interaction.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Polissacarídeos
/
Alfa-Manosidase
/
Fabaceae
Idioma:
En
Revista:
Biochimie
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Japão
País de publicação:
FR
/
FRANCE
/
FRANCIA
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FRANÇA