Work

High‐Throughput Substrate Specificity Studies of Sialidases by Using Chemoenzymatically Synthesized Sialoside Libraries

Year: 2006

Type: article

Abstract: Sialidases, or neuraminidases, are enzymes that cleave terminal sialic acid (Sia) residues from complex sialic acid-containing structures. They have been found in many animals and microorganisms and are important in various physiological and pathological processes. In order to understand the biological significance of diverse sialidases, it is important to study in detail the structural determinants of their natural substrates. Here, we report the synthesis of sialoside libraries containing para-nitrophenol-tagged sialosides with different naturally occurring sialic acid forms, different sialyl linkages, and different penultimate monosaccharides using a highly efficient one-pot three-enzyme chemoenzymatic approach. By using these compounds in a 96-well plate-based colorimetric high-throughput screening platform, the diversity of substrate preference is shown for seven bacterial sialidases. The sialoside libraries and the screening method are convenient tools for unravelling the substrate specificity and the biological function of sialidases.

Source: ChemBioChem

DOI: 10.1002/cbic.200600410

Authors: Harshal A. Chokhawala, Hai Yu, Xi Chen

Institution: University of California, Davis

Language: English

Topic: Carbohydrate Chemistry and Synthesis

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: Mizutani Foundation for Glycoscience, National Institute of General Medical Sciences

Award: Studies of naturally occurring structurally modified carbohydrates