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. 

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

Using heparinase and heparitinase from Flavobacterium heparinum, Buonassisi has provided evidence for the presence of heparan sulfate-containing proteoglycans in the plasma membranes of endothelial cells from rabbit aorta (73.74). 

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. 

Figure 6. Batch fermentation for the production of heparinase by Flavobacterium heparinum on compiex medium. Key , heparinase specific activity A, dry cell weight O, heparin concentration. Reproduced, with permission, from Ref. 15. Copyright 1981, American Society for Microbiology.

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. ... 

Fh, Flavobacterium heparinum Aa, Arthrobacter aurescens Pv, Proteus vulgaris Bs, Bacteroides stercoris Pa, Propionibacterium acnes... 

Fractions obtained from heparin by action of flavobacterium heparinum... 

Fig. 3. Configuration of disaccharide unit in heparin. Above is disaccharide produced by flavobacterium heparinum and below the disaccharide configuration in heparin. (1 - 4)-linked 4-o-(a-L-idopyranosyluronic acid 2-sulfate)-(2-deoxy-2-sulfoamino-a-D-glucopyranosyl 6-sulfate) biose residue. U=uronic acid, A = amino sugar. (After Perlin et al. [15].)...

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

A chondroitinase has been isolated from Flavobacterium heparinum] it acted on chondroitin 6-sulphate to give a tetrasaccharide and an unsaturated, sulphated disaccharide, and on hyaluronic acid to give an unsaturated disaccharide. An en /o-/S-galactosidase from Escherichia freundii hydrolyses /8-D-galacto-pyranosyl linkages, provided that the residues are not sulphated. ... 

Nearest-neighbour analysis has been used to determine the sequences of heparin and heparan sulphates. Structures have been proposed for heparan sulphates A, B, and D based on analysis of the products released by the actions of heparinitase and heparinase from Flavobacterium heparinum. ... 

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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