Chondroitin-sulfate-ABC exolyase

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In enzymology, a chondroitin-sulfate-ABC exolyase (EC 4.2.2.21) is an enzyme that catalyzes the chemical reaction

Exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments

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-sulfate-ABC exolyase. Other names in common use include chondroitinase (ambiguous), chondroitin ABC eliminase (ambiguous), chondroitinase ABC (ambiguous), chondroitin ABC lyase (ambiguous), chondroitin sulfate ABC lyase (ambiguous), ChS ABC lyase (ambiguous), chondroitin sulfate ABC exoeliminase, chondroitin sulfate ABC exolyase, and ChS ABC lyase II.

[edit] References

IUBMB entry for 4.2.2.21
BRENDA references for 4.2.2.21 (Recommended.)
PubMed references for 4.2.2.21
PubMed Central references for 4.2.2.21
Google Scholar references for 4.2.2.21
Yamagata T, Saito H, Habuchi O, Suzuki S (1968). "Purification and properties of bacterial chondroitinases and chondrosulfatases". J. Biol. Chem. 243: 1523–35. PMID 5647268.
Saito H, Yamagata T, Suzuki S (1968). "Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates". J. Biol. Chem. 243: 1536–42. PMID 4231029.
Suzuki S, Saito H, Yamagata T, Anno K, Seno N, Kawai Y, Furuhashi T (1968). "Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion". J. Biol. Chem. 243: 1543–50. PMID 5647269.
Suzuki S (1997). "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides". J. Biol. Chem. 272: 9123–30. doi:10.1074/jbc.272.14.9123. PMID 9083041.
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:10.1111/j.1742-4658.2005.05009.x. PMID 16336265.