biostudies-literaturePeng CJi&apos;nan Science and Technology BureauDepartment of Science and Technology of Shandong ProvinceNational Natural Science Foundation of China (NSFC)Shandong University (SDU)4230-4243https://www.ebi.ac.uk/biostudies/studies/S-EPMC5868263biostudies-literatureUnknown293(12)GlcUAβ1-3GalNAc(4S,6S) (E unit)-rich domains have been shown to play key roles in various biological functions of chondroitin sulfate (CS). However, an enzyme that can specifically isolate such domains through the selective digestion of other domains in polysaccharides has not yet been reported. Here, we identified a glycosaminoglycan lyase from a marine bacterium <i>Vibrio</i> sp. FC509. This enzyme efficiently degraded hyaluronic acid (HA) and CS variants, but not E unit-rich CS-E, into unsaturated disaccharides; therefore, we designated this enzyme a CS-E-resisted HA/CS lyase (HCLase Er). We isolated a series of resistant oligosaccharides from the final product of a low-sulfated CS-E exhaustively digested by HCLase Er and found that the E units were dramatically accumulate in these resiThe Journal of biological chemistryA chondroitin sulfate and hyaluronic acid lyase with poor activity to glucuronyl 4,6-<i>O</i>-disulfated <i>N</i>-acetylgalactosamine (E-type)-containing structures.PMC58682633130066431570071Science and Technology Special Project of Shandong Province 2015zdjs04002Science and Technology Development Project of Shandong Province 2016GGH4502Fundamental Research Funds of Shandong University 2015JC002Independent Innovation Plan of Colleges and Universities in Jinan 201401242Wang QJiao RWang SPeng CLi FHan WWang WfalseA chondroitin sulfate and hyaluronic acid lyase with poor activity to glucuronyl 4,6-<i>O</i>-disulfated <i>N</i>-acetylgalactosamine (E-type)-containing structures.GlcUAβ1-3GalNAc(4S,6S) (E unit)-rich domains have been shown to play key roles in various biological functions of chondroitin sulfate (CS). However, an enzyme that can specifically isolate such domains through the selective digestion of other domains in polysaccharides has not yet been reported. Here, we identified a glycosaminoglycan lyase from a marine bacterium <i>Vibrio</i> sp. FC509. This enzyme efficiently degraded hyaluronic acid (HA) and CS variants, but not E unit-rich CS-E, into unsaturated disaccharides; therefore, we designated this enzyme a CS-E-resisted HA/CS lyase (HCLase Er). We isolated a series of resistant oligosaccharides from the final product of a low-sulfated CS-E exhaustively digested by HCLase Er and found that the E units were dramatically accumulate in these resi2018-01-01T00:00:00Z2018 Mar2025-04-21T22:41:42.988Z2019-06-06T19:11:40ZS-EPMC58682632941478510.1074/jbc.RA117.00123810.1074/jbc.ra117.001238