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RESEARCH & DEVELOPMENT

Enzyme Collections  

Our group’s efforts in the field of molecular biology are directed towards establishing recombinant proteins important in glycobiology and towards developing enzymatic tools for glycan analysis. Our enzymology programs consist largely of enzymes that degrade glycosaminoglycans. These tools have been incorporated into our broader multidisciplinary strategy to analyze glycans. Some of these enzymes are themselves being investigated as therapeutics for human disease.

Heparinase Library

A major research aim of our laboratory is to clone and biochemically characterize a series of HSGAG-degrading enzymes or heparinases. We hope to develop tools for the study of HSGAGs that will facilitate structure-function studies in a manner similar to that in which proteases promoted studies for proteins or restriction enzymes promoted studies for DNA. The heparinases are lyases that depolymerize HSGAGs in a sequence-specific fashion. Three heparinases, heparinases I, II, and III from the soil bacterium Pedobacter heparinus, have been isolated and each cleaves HSGAGs at different sites.

Chondroitinase Library

Similarly, we have sought recombinant versions of enzymes that selectively and uniquely depolymerize chondroitin and dermatan sulfate GAGs, galactosaminoglycans (GalAGs). Our laboratory is home to the most complete library of recombinant and engineered depolymerizing lyases specific for GalAGs in the world.

HSGAG Exo-Enzyme Library

Depolymerizing lyases are useful tools to break a linear polysaccharide chain into constituent oligosaccharide fragments, but complete degradation also requires enzyme activities working at the ends of oligosaccharide chains and at specific sites within disaccharide units that can be differentially modified chemically.

Last Updated: November 29, 2005

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