title: [Lipid-protein interactions: mechanisms of enzymatic glycolipid catabolism and their genetic restrictive escapes].
abstract: Investigations of the genetic basis of ganglioside catabolism have led to the characterisation of two types of lipid-enzyme interaction: a) Breakdown of membrane-bound glycolipids as far as catalysed by membrane-bound enzymes is regulated by the membrane itself. b) The degradation of micelle-forming glycolipids by water-soluble lysosomal enzymes is facilitated by cofactors known as activator proteins. A genetic defect in an activator protein can be just as fatal as the lack of the enzyme itself.
mesh_terms: D000818:Animals; D005732:Gangliosides / Q000378:metabolism; D014644:Genetic Variation; D006017:Glycolipids / Q000378:metabolism*; D006596:Hexosaminidases / Q000378:metabolism; D006801:Humans; D006867:Hydrolases / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008052:Lipid Metabolism, Inborn Errors / Q000201:enzymology*; D008074:Lipoproteins / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology; D008823:Micelles; D009439:Neuraminidase / Q000378:metabolism
chemical_list: D005732:Gangliosides; D006017:Glycolipids; D008074:Lipoproteins; D008823:Micelles; D006867:Hydrolases; D006596:Hexosaminidases; D009439:Neuraminidase
vernacular_title: Lipid-Protein-Wechselwirkungen: Mechanismen des enzymatischen Glykolipid-Abbaus und seine genetisch bedingten Entgleisungen.