Chondroitin-sulfate-ABC endolyase

Endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta₄-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta₄-unsaturated tetra- and disaccharides

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 endolyase. 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 endoeliminase, chondroitin sulfate ABC endolyase, and ChS ABC lyase I.

References

Yamagata T, Saito H, Habuchi O, Suzuki S (1968). "Purification and properties of bacterial chondroitinases and chondrosulfatases". J. Biol. Chem. 243 (7): 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 (7): 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 (7): 1543–50. PMID 5647269.
Suzuki S; Hashimoto, N; Mochizuki, H; Kato, F; Makiguchi, Y; Horie, K; Suzuki, S (1997). "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides". J. Biol. Chem. 272 (14): 9123–30. doi:10.1074/jbc.272.14.9123. PMID 9083041.
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.

Carbon-oxygen lyases (EC 4.2) (primarily dehydratases)

4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase

4.2.2: Acting on polysaccharides	Hyaluronate lyase

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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