Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

Biological properties of N-acyl and N-haloacetyl neuraminic acids: Processing by enzymes of sialic acid metabolism, and interaction with influenza virus

Tools
- Tools
+ Tools

UNSPECIFIED (2002) Biological properties of N-acyl and N-haloacetyl neuraminic acids: Processing by enzymes of sialic acid metabolism, and interaction with influenza virus. BIOORGANIC & MEDICINAL CHEMISTRY, 10 (10). pp. 3175-3185. ISSN 0968-0896

Full text not available from this repository.

Abstract

Several unnatural N-acyl neuraminic acids (N-propionyl, N-hexanoyl, N-benzoyl, N-trifluoroacetyl, N-chloroacetyl, N-difluoroacetyl) were prepared enzymatically using immobilised sialic acid aldolase. N-Trifluoroacetyl- N-chloroacetyl- and N-difluoroacetyl neuraminic acids were shown to enhance up to 10-fold the rate of association of influenza virus A to a sialoglycolipid neomembrane by surface plasmon resonance, and were found to act as weak inhibitors (K-iapp 0.45-2.0 mM) of influenza virus neuraminidase. The N-propionyl, N-chloroacetyl- and N-difluoroacetyl neuraminic acids were found to be substrates for recombinant Escherichia coli CMP sialate synthase, to give the corresponding CMP-N-acyl-neuraminic acids. CMP-N-propionyl neuraminic acid was found not to be a substrate for CMP-N-acetyl neuraminic acid hydroxylase from pig submandibular gland. (C) 2002 Elsevier Science Ltd. All rights reserved.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Journal or Publication Title: BIOORGANIC & MEDICINAL CHEMISTRY
Publisher: PERGAMON-ELSEVIER SCIENCE LTD
ISSN: 0968-0896
Date: October 2002
Volume: 10
Number: 10
Number of Pages: 11
Page Range: pp. 3175-3185
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/10590

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

Email us: publications@warwick.ac.uk
Contact Details
About Us