High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries.

High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Research Abstract Details 

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High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Abstract Text:

Harshal A Chokhawala,Hai Yu,Xi Chen,

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.

High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Publishing Authors By Initials

HA Chokhawala,H Yu,X Chen,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Chembiochem : a European journal of chemical biolo

VOLUME: 8

Page Numbers: 194-201

Journal Abbreviation: Chembiochem

ISSN: 1439-4227

DAY: 22

MONTH: Jan

YEAR: 2007

High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 100937360

High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: metabolism

Chemical & Substance for Abstract: High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Information

Substance Name: Neuraminidase

Registry Number: EC 3.2.1.18

Grant and Affiliation Information for High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries.

AFFILIATION: Department of Chemistry, University of California, Davis, One Shields Avenue, Davis, CA 95616, USA.

Country: Germany

AGENCY: United States NIGMS

GRANT: R01GM076360

ACRONYM: GM

MEDLINETA: Chembiochem

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