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Chondroitin ABC lyase

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chondroitin-sulfate-ABC endolyase
Identifiers
EC no.4.2.2.20
CAS no.9024-13-9
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BRENDABRENDA entry
ExPASyNiceZyme view
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MetaCycmetabolic pathway
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chondroitin-sulfate-ABC exolyase
Identifiers
EC no.4.2.2.21
CAS no.9024-13-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Chondroitin ABC lyase (EC 4.2.2.20 EC 4.2.2.21, chondroitinase, chondroitin ABC eliminase, chondroitinase ABC) is an enzyme with systematic name chondroitin ABC lyase.[1][2] This enzyme catalyses the following chemical reaction

Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups

This enzyme acts on chondroitin 4-sulfate, chondroitin 6-sulfate and dermatan sulfate.

Uses

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Following a spinal cord injury, this enzyme can be used to erode scar tissue that can interfere with regeneration.[3]

References

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  1. ^ Yamagata T, Saito H, Habuchi O, Suzuki S (April 1968). "Purification and properties of bacterial chondroitinases and chondrosulfatases". The Journal of Biological Chemistry. 243 (7): 1523–35. doi:10.1016/S0021-9258(18)93574-X. PMID 5647268.
  2. ^ Saito H, Yamagata T, Suzuki S (April 1968). "Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates". The Journal of Biological Chemistry. 243 (7): 1536–42. doi:10.1016/S0021-9258(18)93575-1. PMID 4231029.
  3. ^ Bartus K, James ND, Didangelos A, Bosch KD, Verhaagen J, Yáñez-Muñoz RJ, Rogers JH, Schneider BL, Muir EM, Bradbury EJ (April 2014). "Large-scale chondroitin sulfate proteoglycan digestion with chondroitinase gene therapy leads to reduced pathology and modulates macrophage phenotype following spinal cord contusion injury". The Journal of Neuroscience. 34 (14): 4822–36. doi:10.1523/JNEUROSCI.4369-13.2014. PMC 3972714. PMID 24695702.
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