Specificity of flavobacterial glycuronidases acting on disaccharides derived from glycosaminoglycans.
The specificity of the unusual flavobacterial glycuronidases that act on disaccharides containing delta4,5-unsaturated uronic acids was reinvestigated. The results show that the enzyme that hydrolyses the uronidic bond in disaccharides from hyaluronic acid and the chondroitin sulphates appears to be mainly specific for beta-D-(1 leads to 3)-derived linkages. The enzyme that hydrolyses the uronidic bond in a variety of disaccharides obtained from heparan sulphate and heparin appears to be specific for beta-D-(1 leads to 4)- and alpha-L-(1 leads to 4)- derived linkages. Thus the glycuronidases seem to be specific for linkage position rather than anomeric configuration, as had been thought previously. In addition, the data confirm other evidence that the major glucuronidic linkages in heparan sulphate and heparin have the beta-D-configuration, and the iduronidic linkages the alpha-L-configuration.
D002809:Chondroitin Sulfates / Q000378:metabolism; D004187:Disaccharides / Q000378:metabolism*; D005417:Flavobacterium / Q000201:enzymology*; D005966:Glucuronidase / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism; D006497:Heparan Sulfate / Q000378:metabolism; D006820:Hyaluronic Acid / Q000378:metabolism
D002809:Chondroitin Sulfates; D004187:Disaccharides; D005966:Glucuronidase; D006025:Glycosaminoglycans; D006493:Heparin; D006497:Heparan Sulfate; D006820:Hyaluronic Acid