Carissa L. White coauthored a 2002 study identifying a heparosan synthase. The characterized glycosyltransferase combined two sugar-transfer activities in one protein, building a heparosan chain from glucuronic acid and N-acetylglucosamine units. The product was the unsulfated, unepimerized backbone related to heparin, rather than a fully modified heparin molecule.[ref]
Identification and molecular cloning of a heparosan synthase from Pasteurella multocida type D by P. L. DeAngelis and Carissa L. White. Abstract, Journal of Biological Chemistry 277 (2002), pp. 7209–7213; DOI 10.1074/jbc.M112130200.
The study tested which nucleotide sugars supported chain formation and compared the product's susceptibility to different polysaccharide-cleaving enzymes. An illuminating distinction is between building a repeating backbone and modifying that backbone: identifying a heparosan synthase establishes a particular polymerization activity, but does not establish all the later reactions needed to make a differently substituted glycosaminoglycan. The reported one-protein, two-activity mechanism also shows that two alternating chemical additions need not require two separate polypeptides.[ref]
Identification and molecular cloning of a heparosan synthase from Pasteurella multocida type D by P. L. DeAngelis and Carissa L. White. Abstract: dual-action transferase, donor specificity and product digestion.
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