4.2.2.21: chondroitin-sulfate-ABC exolyase

This is an abbreviated version!
For detailed information about chondroitin-sulfate-ABC exolyase, go to the full flat file.

Word Map on EC 4.2.2.21

4.2.2.21

glycosaminoglycans

articular

dermatan

tensile

4-sulfated

chabc

neocartilage

fibrocartilage

perineuronal

chondroitinase-ac

oversulfated

l-iduronic

neurocan

analysis

medicine

galactosaminoglycans

chondroitin-4-sulfate

synthesis

biotechnology

Reaction

2-(acetylamino)-2-deoxy-3-O-alpha-L-threo-hex-4-enopyranuronosyl-4-O-sulfo-beta-D-galactopyranose

Synonyms

BactnABC, cABCII, chABC, Chondroitin Sulfate Lyase ABC, chondroitinase ABC, chondroitinase ABC II, chondroitinase AC, chondroitinase ACII, chondroitinase-ABC, ChS ABC lyase II, EC 4.2.2.4, EC 4.2.99.6, HCLase

ECTree

4 Lyases

4.2 Carbon-oxygen lyases

4.2.2 Acting on polysaccharides

4.2.2.21 chondroitin-sulfate-ABC exolyase

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Results	in table
3	Activating Compound
20	AA Sequence
9	Application
4	Cloned(Commentary)
1	Crystallization (Commentary)
2	General Stability
16	Inhibitors
7	kcat/KM [mM/s]
56	KM Value [mM]
1	Localization
8	Metals/Ions
11	Molecular Weight [Da]
31	Organism
4	Pathway
2	PDB ID
17	pH Optimum
2	pH Range
5	pI Value
45	Protein Variants
8	Purification (Commentary)
3	Reaction
28	Reference
1	Source Tissue
21	Specific Activity [micromol/min/mg]
2	Storage Stability
88	Substrates and Products (Substrate)
7	Subunits
22	Synonyms
1	Systematic Name
11	Temperature Optimum [°C]
2	Temperature Range [°C]
4	Temperature Stability [°C]
55	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.2.2.21 - chondroitin-sulfate-ABC exolyase

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crystal structure identifies additional structurally conserved residues potentially involved in catalysis. A conserved cluster located 12 A from the catalytic tetrad is shown. A His in this cluster is essential for catalysis of dermatane sulfate but not chondroitin sulfate. The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together

Bacteroides thetaiotaomicron

Q8A2I1

692529