Heparin lyase
In enzymology, a heparin lyase (EC 4.2.2.7) is an enzyme that catalyzes the chemical reaction
- Eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is heparin lyase. Other names in common use include heparin eliminase, and heparinase.
There are 3 main producers of heparinase,Aglyco, Iduron and Ibex.
References
- Hovingh P, Linker A (1970). "The enzymatic degradation of heparin and heparitin sulfate. 3 Purification of a heparitinase and a heparinase from flavobacteria". J. Biol. Chem. 245 (22): 6170–5. PMID 5484472.
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|