Chondroitin B lyase – Wikipedia

The enzyme chondroitin B lyase (EC 4.2.2.19) catalyzes the following process:

Eliminative cleavage of dermatan sulfate containing (1→4)-β-D-hexosaminyl and (1→3)-β-D-glucurosonyl or (1→3)-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (ΔUA-GalNAc-4S).

Glossary:

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is chondroitin B lyase. Other names in common use include chondroitinase B, ChonB, and ChnB.

References[edit]

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• Pojasek K, Raman R, Kiley P, Venkataraman G, Sasisekharan R (2002). “Biochemical characterization of the chondroitinase B active site”. J. Biol. Chem. 277 (34): 31179–86. doi:10.1074/jbc.M201552200. PMID 12063249.
• Pojasek K, Shriver Z, Kiley P, Venkataraman G, Sasisekharan R (2001). “Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum”. Biochem. Biophys. Res. Commun. 286 (2): 343–51. doi:10.1006/bbrc.2001.5380. PMID 11500043.
• Suzuki K, Terasaki Y, Uyeda M (2002). “Inhibition of hyaluronidases and chondroitinases by fatty acids”. J. Enzyme. Inhib. Med. Chem. 17 (3): 183–6. doi:10.1080/14756360290032930. PMID 12443044.
• Ototani N, Yosizawa Z (1979). “Purification of chondroitinase B and chondroitinase C using glycosaminoglycan-bound AH-Sepharose 4B”. Carbohydr. Res. 70 (2): 295–306. doi:10.1016/S0008-6215(00)87109-8. PMID 427837.
• K, Zimmermann JJ; Su H (2000). “Isolation and Expression in Escherichia coli of cslA and cslB, Genes Coding for the Chondroitin Sulfate-Degrading Enzymes Chondroitinase AC and Chondroitinase B, Respectively, from Flavobacterium heparinum”. Appl. Environ. Microbiol. 66 (1): 29–35. doi:10.1128/AEM.66.1.29-35.2000. PMC 91781. PMID 10618199.
• V, Sasisekharan R, Cygler M (2004). “The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic machinery”. J. Biol. Chem. 279 (31): 32882–96. doi:10.1074/jbc.M403421200. PMC 4135467. PMID 15155751.
• Li Y, Matte A, Su H, Cygler M (1999). “Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum”. Acta Crystallogr. D. 55 (Pt 5): 1055–7. doi:10.1107/S0907444999002097. PMID 10216304.
• Huang W, Matte A, Li Y, Kim YS, Linhardt RJ, Su H, Cygler M (1999). “Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 A resolution”. J. Mol. Biol. 294 (5): 1257–69. doi:10.1006/jmbi.1999.3292. PMID 10600383.
• Lauder RM; Nieduszynski, IA; Giannopoulos, M; Weeks, SD; Sadler, IH; Lauder, RM (2005). “Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides”. FEBS J. 272 (24): 6276–86. doi:10.1111/j.1742-4658.2005.05009.x. PMID 16336265.