Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 25, Pages 20996-21002Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.359885
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Funding
- National Institutes of Health [AI50050, HL094463, GM072667]
- National Science Foundation [CHE-1111550]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1111550] Funding Source: National Science Foundation
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Heparan sulfate (HS), a highly sulfated polysaccharide, is biosynthesized through a pathway involving several enzymes. C-5-epimerase (C-5-epi) is a key enzyme in this pathway. C-5-epi is known for being a two-way catalytic enzyme, displaying a reversible catalytic mode by converting a glucuronic acid to an iduronic acid residue, and vice versa. Here, we discovered that C-5-epi can also serve as a one-way catalyst to convert a glucuronic acid to an iduronic acid residue, displaying an irreversible catalytic mode. Our data indicated that the reversible or irreversible catalytic mode strictly depends on the saccharide substrate structures. The biphasic mode of C-5-epi offers a novel mechanism to regulate the biosynthesis of HS with the desired biological functions.
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