Chondroitin AC lyase
From Wikipedia, the free encyclopedia
In enzymology, a chondroitin AC lyase (EC 4.2.2.5) is an enzyme that catalyzes the chemical reaction
- Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-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.
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[edit] 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.
[edit] References
- IUBMB entry for 4.2.2.5
- BRENDA references for 4.2.2.5 (Recommended.)
- PubMed references for 4.2.2.5
- PubMed Central references for 4.2.2.5
- Google Scholar references for 4.2.2.5
- NAKADA HI, WOLFE JB (1961). "Studies on the enzyme chondroitinase: product structure and ion effects". Arch. Biochem. Biophys. 94: 244–51. doi: . PMID 13727579.
- 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: 343–51. doi: . PMID 11500043.
- Cygler M (Pt 2). "Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum". Acta. Crystallogr. D. Biol. Crystallogr. 54: 279–80. doi: . PMID 9761894.
- 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: 6276–86. doi: . PMID 16336265.
[edit] External links
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- The CAS registry number for this enzyme class is 9047-57-8.