The core-specific lysosomal alpha(1-6)-mannosidase activity depends on aspartamidohydrolase activity.
The substrate specificity of the core-specific rat liver lysosomal alpha(1-6)-mannosidase was investigated using mannosylated oligosaccharides and glycoasparagines. Hydrolysis of Man(alpha 1-6) linkage hydrolysis was demonstrated to follow the action of endoglycosidases, namely aspartyl-N-acetyl-beta-D-glucosaminidase and endo-N-acetyl-beta-D-glucosaminidase. The results are discussed with respect to the nature of the carbohydrate materials stored in the tissues and excreted in the urine from patients suffering from aspartylglucosaminuria and fucosidosis.
Haeuw
J F
JF
Unité Mixte de Recherche du CNRS no. 111, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.
Grard
T
T
Alonso
C
C
Strecker
G
G
Michalski
J C
JC
D000107:Acetylation; D000818:Animals; D001227:Aspartylglucosylaminase / Q000378:metabolism; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D008361:Mannosidases / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity
D006020:Glycopeptides; D009844:Oligosaccharides; C007872:glycoasparagines; D008361:Mannosidases; C078166:alpha(1-6)mannosidase; D001227:Aspartylglucosylaminase