EC 4.2.2.20 - Chondroitin-sulfate-ABC endolyase

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IntEnz Enzyme Nomenclature
EC 4.2.2.20

Names

Accepted name:
chondroitin-sulfate-ABC endolyase
Other names:
chondroitin ABC eliminase [ambiguous]
chondroitin sulfate ABC lyase [ambiguous]
chondroitinase ABC [ambiguous]
chondroitinase [ambiguous]
chondroitin ABC lyase [ambiguous]
ChS ABC lyase [ambiguous]
chondroitin sulfate ABC endoeliminase
chondroitin sulfate ABC endolyase
ChS ABC lyase I
Systematic name:
chondroitin-sulfate-ABC endolyase

Reaction

Comments:

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(β1-3)GalNAc(β1-]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(α1-3)GalNAc(β1-]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].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0034000
UniProtKB/Swiss-Prot:

References

  1. Yamagata, T., Saito, H., Habuchi, O. and Suzuki, S.
    Purification and properties of bacterial chondroitinases and chondrosulfatases.
    J. Biol. Chem. 243 : 1523-1535 (1968). [PMID: 5647268]
  2. Saito, H., Yamagata, T. and Suzuki, S.
    Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates.
    J. Biol. Chem. 243 : 1536-1542 (1968). [PMID: 4231029]
  3. Suzuki, S., Saito, H., Yamagata, T., Anno, K., Seno, N., Kawai, Y. and Furuhashi, T.
    Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion.
    J. Biol. Chem. 243 : 1543-1550 (1968). [PMID: 5647269]
  4. Hamai, A., Hashimoto, N., Mochizuki, H., Kato, F., Makiguchi, Y., Horie, K. and Suzuki, S.
    Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides.
    J. Biol. Chem. 272 : 9123-9130 (1997). [PMID: 9083041]
  5. Huckerby, T.N., Nieduszynski, I.A., Giannopoulos, M., Weeks, S.D., Sadler, I.H. and Lauder, R.M.
    Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides.
    FEBS J. 272 : 6276-6286 (2005). [PMID: 16336265]

[EC 4.2.2.20 created 2006 (EC 4.2.2.4 created 1972, part-incorporated 2006 (EC 4.2.99.6 created 1965, part-incorporated 1976)]