Chondroitinase C from Flavobacterium heparinum.
A chondroitinase that acts upon chondroitin sulfate C and hyaluronic acid was isolated from Flavobacterium heparinum. This enzyme was seperated from constitutional chondroitinase AC and an induced chondroitinase B also present in extracts of F. heparinum previously grown in the presence of chondroitin sulfates A, B or C. The enzyme acts upon chondroitin sulfate C producing tetrasaccharide plus an unsaturated 6-sulfated disaccharide (delta Di-6S), and upon hyaluronic acid producing unsaturated nonsulfated disaccharide (delta Di-OS). Chondroitin sulfate A is also degraded producing oligosaccharides and delta Di-6S but not delta Di-4S. The chondroitinase C is also distinguished from the chondroitinases B and AC by several properties, such as effect of ions, temperature for optimal activity, and susceptibility to increasing salt concentrations. The substrate specificity of the chondroitinase C is different from that of any other chondroitinase or hyaluronidase described so far.
D002809:Chondroitin Sulfates / Q000378:metabolism; D002810:Chondroitinases and Chondroitin Lyases / Q000302:isolation & purification / Q000378:metabolism*; D004187:Disaccharides / Q000032:analysis; D005417:Flavobacterium / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009994:Osmolar Concentration; D010710:Phosphates / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013329:Structure-Activity Relationship
D004187:Disaccharides; D010710:Phosphates; D012965:Sodium Chloride; D002809:Chondroitin Sulfates; D002810:Chondroitinases and Chondroitin Lyases