The core-specific lysosomal alpha(1-6)-mannosidase activity depends on aspartamidohydrolase activity

Biochem J. 1994 Feb 1;297 ( Pt 3)(Pt 3):463-6. doi: 10.1042/bj2970463.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Aspartylglucosylaminase / metabolism
  • Carbohydrate Sequence
  • Glycopeptides / metabolism
  • Lysosomes / enzymology*
  • Mannosidases / metabolism*
  • Mass Spectrometry
  • Molecular Sequence Data
  • Oligosaccharides / metabolism
  • Rats
  • Substrate Specificity

Substances

  • Glycopeptides
  • Oligosaccharides
  • glycoasparagines
  • Mannosidases
  • alpha(1-6)mannosidase
  • Aspartylglucosylaminase