Chondroitin ABC lyase

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Chondroitin ABC lyase (EC 4.2.2.4, 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.

References

↑ Yamagata, T., Saito, H., Habuchi, O. and Suzuki, S. (1968). "Purification and properties of bacterial chondroitinases and chondrosulfatases". J. Biol. Chem. 243: 1523–1535. PMID 5647268.
↑ Saito, H., Yamagata, T. and Suzuki, S. (1968). "Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates". J. Biol. Chem. 243: 1536–1542. PMID 4231029.

External links

Chondroitin ABC lyase at the US National Library of Medicine Medical Subject Headings (MeSH)

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

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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