A TRUNCATED ALPHA-2-3-SIALYLTRANSFERASE FOR THE SYNTHESIS OF SIALOSIDES AND SIALYL GLYCOLIPIDS
University of California System: University of California, Davis - UC Davis
posted on 12/09/2011
Researchers at the University of California, Davis have developed a truncated sialyltransferase that is a valuable catalyst for synthesizing sialosides with or without a lipid portion.
Suggested Uses
Useful for:
· Catalyzing the synthesis of:
o Sialosides
o Sialyl glycolipids
Advantages
- PmST3 enzyme:
- Highly soluble: capable of utilizing substrates (e.g. oligosaccharides, glycolipids) with or without lipid chains
- Excellent for use in enzymatic synthesis: lacks sialidase activity
Detailed Description
Sialic acids are a family of monosaccharides that are commonly found as terminal residues on cell surface glycoproteins/glycolipids of higher animals. They have a vital role in cellular communication and recognition.To a much lesser degree, they are also found in microorganisms and their presence is often linked with pathogenicity.
Pasteurella multocida alpha-2-3-sialyltransferase 3 (PmST3) is a powerful catalyst that is useful for synthesizing sialosides and sialyl glycolipids. UC Davis researchers have discovered that by truncating the carboxyl terminus of PmST3, the truncated enzyme (PmST3delta35) is more soluble and shows high expression in E. coli expression system. Truncated PmST3 catalyzes the transfer of activated sialic acids to the appropriate acceptors, resulting in the formation of alpha-2-3-linked sialosides with or without a lipid portion.
File Number: 22187
| Copyright: | ©2011, The Regents of the University of California |
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This innovation currently is not available for online licensing. Please contact Madhu Sharma at University of California System: University of California, Davis - UC Davis for more information.
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