Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM). Endolytic cleavage of (1->4)-beta-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta(4)-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta(4)-unsaturated tetra- and disaccharides. Is inhibited by Zn(2+), Ni(2+), Fe(2+) and Cu(2+). Optimum pH is 8. Is essentially inactive at pH 9.0. Optimum temperature is 37 degrees Celsius. Monomer. By chondroitin sulfate or its degraded products. Consists of three domains. The middle domain contains the catalytic site in a wide-open cleft. Belongs to the polysaccharide lyase 8 family. PubMed:7512814 shows amino acid differences at positions 317, 321, 410, 694, 738 and 866 due to incorrect translation of the nucleotide sequence.