Flavobacterium heparinum lyases

This compound was designed as potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum, useful for the structural analysis of the enzyme active site. 

Lohse DL, Linhardt RJ (1992) Purification and characterization of heparin lyases from Flavobacterium heparinum. J Biol Chem 267 24347-55. 

PL 9 - Both chondroitin and alginate lyase. PL 9 contains both M-M alginate lyases and chondroitin lyases, which both catalyse syn eliminations. The one structure available (that of a chondroitinase from Flavobacterium heparinum) is of a helix of p-strands typical of enzymes acting on pectate, although three short a-helices are also in the structure. Despite the existence of a complex with —2 and —1 sites occupied, assignment of catalytic groups is speculative. 

The Linhardt laboratory prepares polysaccharide lyases from Flavobacterium heparinum and Bacteroides stearcoris. These enzymes have been purified to homogeneity, cloned, and expressed in bacteria. Their physical and catalytic properties and specificity have been extensively investigated. ... 

An enzyme that hydrolyses dermatan sulphate, but neither chondroitin 4-sulphate nor chondroitin 6-sulphate, has been isolated from Flavobacterium heparinum grown in the presence of glycosaminoglycans. Chondroitin and dermatan sulphates and disaccharides obtained from them induced the synthesis of this enzyme, which was separated from a chondroitin sulphate lyase AC. The enzyme acted on dermatan sulphate to give an unsaturated, sulphated disaccharide and higher oligosaccharides. 

Heparin Lyases and Heparan Sulphate Lyases The isolation and partial characterization of a heparin lyase and two heparan sulphate lyases from Flavobacterium heparinum have been reported. ... 

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