Enzymes Flavobacterium heparinum

Extracts of Flavobacterium heparinum that had been induced to grow on heparin-like polysaccharides contain a number of enzymes that may ultimately degrade heparin and heparan sulfate to monosaccharides.137,145 240 The enzymes that cause the primary cleavage of heparinlike chains are heparinase (EC 4.2.2.7) and heparanase (EC 4.2.2.8, formerly called heparitinase241,242). 

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

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. ... 

Dietrich, C. P. Studies on the Induction of Heparin Degrading Enzymes in Flavobacterium Heparinum Biochemistry 8, 3342-3347 (1969). 

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. 

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