chondroitin-sulfate-ABC endolyase;
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;
ChS ABC lyase I

Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides

chondroitin-sulfate-ABC endolyase

Endolytic cleavage of (1->4)-beta-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 degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [5]. The related enzyme EC 4.2.2.21, chondroitin-sulfate-ABC exolyase, has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20 [4].

1  [PMID:5647268]

Yamagata T, Saito H, Habuchi O, Suzuki S.

Purification and properties of bacterial chondroitinases and chondrosulfatases.

J. Biol. Chem. 243 (1968) 1523-35.

Proteus vulgaris, Flavobacterium heparinum

2  [PMID:4231029]

Saito H, Yamagata T, Suzuki S.

Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates.

J. Biol. Chem. 243 (1968) 1536-42.

Proteus vulgaris, Flavobacterium heparinum

3  [PMID:5647269]

Suzuki S, Saito H, Yamagata T, Anno K, Seno N, Kawai Y, Furuhashi T.

Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion.

J. Biol. Chem. 243 (1968) 1543-50.

Proteus vulgaris, Flavobacterium heparinum

4  [PMID:9083041]

Hamai A, Hashimoto N, Mochizuki H, Kato F, Makiguchi Y, Horie K, Suzuki S.

Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides.

J. Biol. Chem. 272 (1997) 9123-30.

Proteus vulgaris

5  [PMID:16336265]

Huckerby TN, Nieduszynski IA, Giannopoulos M, Weeks SD, Sadler IH, Lauder RM.

Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides.

FEBS. J. 272 (2005) 6276-86.

Proteus vulgaris