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Sismey-Ragatz, Alison E., Green, Dixy E., Otto, Nigel J., Rejzek, Martin, Field, Robert A. 
ORCID: https://orcid.org/0000-0001-8574-0275 and DeAngelis, Paul L.
(2007)
Chemoenzymatic synthesis with distinct Pasteurella heparosan synthases:Monodisperse polymers and unnatural structures.
Journal of Biological Chemistry, 282 (39).
pp. 28321-28327.
ISSN 0021-9258
Abstract
Heparosan (-GlcUA-β1,4-GlcNAc-α1,4-)n is a member of the glycosaminoglycan polysaccharide family found in the capsule of certain pathogenic bacteria as well as the precursor for the vertebrate polymers, heparin and heparan sulfate. The two heparosan synthases from the Gram-negative bacteria Pasteurella multocida, PmHS1 and PmHS2, were efficiently expressed and purified using maltose-binding protein fusion constructs. These relatively homologous synthases displayed distinct catalytic characteristics. PmHS1, but not PmHS2, was able to produce large molecular mass (100-800 kDa) monodisperse polymers in synchronized, stoichiometrically controlled reactions in vitro. PmHS2, but not PmHS1, was able to utilize many unnatural UDP-sugar analogs (including substrates with acetamido-containing uronic acids or longer acyl chain hexosamine derivatives) in vitro. Overall these findings reveal potential differences in the active sites of these two Pasteurella enzymes. In the future, these catalysts should allow the creation of a variety of heparosan and heparinoids with utility for medical applications.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Chemistry, Pharmacy and Pharmacology Faculty of Science > School of Biological Sciences |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 06 Sep 2024 13:35 |
| Last Modified: | 25 Sep 2024 18:07 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96608 |
| DOI: | 10.1074/jbc.M701599200 |
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