Biology:Chondroitin AC lyase

From HandWiki
chondroitin AC lyase
Identifiers
EC number4.2.2.5
CAS number9047-57-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

The enzyme chondroitin AC lyase (EC 4.2.2.5) catalyzes the chemical reaction

Eliminative degradation of polysaccharides containing 1,4-β-D-hexosaminyl and 1,3-β-D-glucuronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups

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 AC lyase. Other names in common use include chondroitinase (ambiguous), chondroitin sulfate lyase, chondroitin AC eliminase, chondroitin AC lyase, chondroitinase AC, and ChnAC.

Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1CB8, 1HM2, 1HM3, 1HMU, 1HMW, 1RW9, 1RWA, 1RWC, 1RWF, 1RWG, and 1RWH.

References

  • "Studies on the enzyme chondroitinase: product structure and ion effects". Arch. Biochem. Biophys. 94 (2): 244–51. 1961. doi:10.1016/0003-9861(61)90037-6. PMID 13727579. 
  • "Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum". Biochem. Biophys. Res. Commun. 286 (2): 343–51. 2001. doi:10.1006/bbrc.2001.5380. PMID 11500043. 
  • Cygler M; Shilton, BH; Li, Y; Allaire, M; Laliberté, M; Eggimann, B; Cygler, M (1998). "Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum". Acta Crystallogr. D 54 (Pt 2): 279–80. doi:10.1107/S0907444997009037. PMID 9761894. 
  • 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.