Chondroitin AC lyase

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chondroitin AC lyase
chondroitin AC lyase
Identifiers
EC no.	4.2.2.5
CAS no.	9047-57-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Last updated March 11, 2025

The enzyme chondroitin AC lyase (EC 4.2.2.5) catalyzes the chemical reaction

Eliminative degradation of polysaccharides containing 1,4-β-D-hexosaminyl and 1,3-β-D-glucuronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups

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 AC lyase. Other names in common use include chondroitinase (ambiguous), chondroitin sulfate lyase, chondroitin AC eliminase, chondroitin AC lyase, chondroitinase AC, and ChnAC.

Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1CB8, 1HM2, 1HM3, 1HMU, 1HMW, 1RW9, 1RWA, 1RWC, 1RWF, 1RWG, and 1RWH.

References

NAKADA HI, WOLFE JB (1961). "Studies on the enzyme chondroitinase: product structure and ion effects". Arch. Biochem. Biophys. 94 (2): 244–51. doi:10.1016/0003-9861(61)90037-6. PMID 13727579.
Pojasek K, Shriver Z, Kiley P, Venkataraman G, Sasisekharan R (2001). "Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum". Biochem. Biophys. Res. Commun. 286 (2): 343–51. doi:10.1006/bbrc.2001.5380. PMID 11500043.
Cygler M; Shilton, BH; Li, Y; Allaire, M; Laliberté, M; Eggimann, B; Cygler, M (1998). "Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum". Acta Crystallogr. D . 54 (Pt 2): 279–80. Bibcode:1998AcCrD..54..279F. doi:10.1107/S0907444997009037. PMID 9761894.
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. S2CID 40325628.

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v t e 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 Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)