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Review
. 2006:53:187-215.
doi: 10.1016/S1054-3589(05)53009-6.

CS lyases: structure, activity, and applications in analysis and the treatment of diseases

Robert J Linhardt  1 , Fikri Y Avci, Toshihiko Toida, Yeong Shik Kim, Miroslaw Cygler
Affiliations
Review

CS lyases: structure, activity, and applications in analysis and the treatment of diseases

Robert J Linhardt et al. Adv Pharmacol. 2006.
No abstract available

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Figures

FIGURE 1
FIGURE 1
CS, oversulfated CS and chondroitin: the molecular weight ranges from 5000–50,000 (average 25 kDa). DS and oversulfated DS: the molecular weight ranges from 5000–50,000 (average 25 kDa).
FIGURE 2
FIGURE 2
Mechanism for the enzymatic breakdown of GAGs. Lyases catalyze eliminative cleavage and hydrolases catalyze hydrolytic cleavage leading to different oligosaccharide products.
FIGURE 3
FIGURE 3
Comparison of crystal structures of chondroitinases PvulABCI (left), FlavoAC (center), and FlavoB (right).
FIGURE 4
FIGURE 4
Chondroitin-4,6-sulfate tetrasaccharide in the active site of FlavoAC Tyr234Phe mutant.
FIGURE 5
FIGURE 5
Experimental electron density map of the active site region of ArthroAC. Green contours are drawn at 3σ level, red contours at 5σ level. In the native structure, there is a phosphate ion in the active site. Nitrogen atoms are blue, oxygens are red, carbons are gray, and phosphorus is yellow.
FIGURE 6
FIGURE 6
Conformation of the chondroitin-4-sulfate tetrasaccharide substrate bound in the active site of ArthroAC. Omit electron density map is drawn at the 3σ level.
FIGURE 7
FIGURE 7
Enzymatic depolymerization of chondroitin O-methyl ester.
FIGURE 8
FIGURE 8
Three disaccharide products bound in the active site of chondroitinase B. Bound calcium atom is shown as a yellow sphere, two water molecules as red spheres.
FIGURE 9
FIGURE 9
The superposition of the active-site tetrad of FlavoAC and PvulABCI. The Asn175 of FlavoAC and Arg500 of PvulABCI are also shown.
FIGURE 10
FIGURE 10
The disposition of the substrate in FlavoAC (left) was transferred to PvulABCI (right) based on the superposition of the active site tetrad. In this open form of PvulABCI are very few contacts between the enzyme and its substrate.
FIGURE 11
FIGURE 11
Controlled enzymatic depolymerization of DS by chondroitinase ABC and mercuric acetate treatment to remove the unsaturated nonreducing end residue.
FIGURE 12
FIGURE 12
Preparation of desulfated and sulfoprotected disaccharide starting materials for the synthesis of CS/DS/HA oligosaccharides.
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