EC                 Enzyme                                 

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
Carbon-oxygen lyases;
Acting on polysaccharides
BRITE hierarchy
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, 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].
EC created 2006 (EC created 1972, part-incorporated 2006 (EC created 1965, part incorporated 1976))
K08961  chondroitin-sulfate-ABC endolyase/exolyase
SES: SARI_02380
YPE: YPO0824
YPK: y3211
YPH: YPC_0996
YPA: YPA_0445
YPN: YPN_3027
YPM: YP_2832
YPG: YpAngola_A3277
YPZ: YPZ3_0887
YPD: YPD4_0844
YPX: YPD8_0842
YPW: CH59_1039
YPV: BZ15_2750
YPL: CH46_92
YPO: BZ17_3545
YPY: YPK_0997
YPB: YPTS_3194
YPQ: DJ40_3406
YPU: BZ21_2390
YPR: BZ20_3090
YPC: BZ23_2669
YPF: BZ19_2453
YRU: BD65_2433
ARM: ART_3703
SRO: Sros_2256
AGL: PYTT_0964
PBAS: SMSP2_01417(chonabc_1) SMSP2_01425(chonabc_2)
BTHO: Btheta7330_04950(chonabc_1) Btheta7330_04976(chonabc_2)
BOA: Bovatus_03443(chonabc_1) Bovatus_03480(chonabc_2)
PHE: Phep_0784
 » show all
1  [PMID:5647268]
Yamagata T, Saito H, Habuchi O, Suzuki S.
Purification and properties of bacterial chondroitinases and chondrosulfatases.
J Biol Chem 243:1523-35 (1968)
2  [PMID:4231029]
Saito H, Yamagata T, Suzuki S.
Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates.
J Biol Chem 243:1536-42 (1968)
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 243:1543-50 (1968)
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 272:9123-30 (1997)
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 272:6276-86 (2005)
Other DBs
ExplorEnz - The Enzyme Database:
IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 9024-13-9

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