Repository logo
  • Log In
    New user? Click here to register.Have you forgotten your password?
University College Dublin
  • Colleges & Schools
  • Statistics
  • All of DSpace
  • Log In
    New user? Click here to register.Have you forgotten your password?
  1. Home
  2. College of Science
  3. School of Biomolecular & Biomedical Science
  4. Biomolecular and Biomedical Science Research Collection
  5. Redesign of Polyene Macrolide Glycosylation: Engineered Biosynthesis of 19-(O)-Perosaminyl-Amphoteronolide B
 
  • Details
Options

Redesign of Polyene Macrolide Glycosylation: Engineered Biosynthesis of 19-(O)-Perosaminyl-Amphoteronolide B

File(s)
FileDescriptionSizeFormat
Download CB_accepted_manuscript-D-09-00238R1.pdf642.84 KB
Author(s)
Hutchinson, Eve 
Murphy, Barry 
Dunne, Terence 
Breen, Ciaran 
Rawlings, Bernard 
Caffrey, Patrick 
Uri
http://hdl.handle.net/10197/8287
Date Issued
26 February 2010
Date Available
20T10:42:53Z January 2017
Abstract
Most polyene macrolide antibiotics are glycosylated with mycosamine (3,6-dideoxy-3-aminomannose). In the amphotericin B producer, Streptomyces nodosus, mycosamine biosynthesis begins with AmphDIII-catalysed conversion of GDP-mannose to GDP-4-keto-6-deoxymannose. This is converted to GDP-3-keto-6-deoxymannose, which is transaminated to mycosamine by the AmphDII protein. The glycosyltransferase AmphDI transfers mycosamine to amphotericin aglycones (amphoteronolides). The aromatic heptaene perimycin is unusual among polyenes in that the sugar is perosamine (4,6-dideoxy-4-aminomannose), which is synthesised by direct transamination of GDP-4-keto-6-deoxymannose. Here we use the Streptomyces aminophilus perDII perosamine synthase and perDI perosaminyltransferase genes to engineer biosynthesis of perosaminyl-amphoteronolide B in S. nodosus. Efficient production required a hybrid glycosyltransferase containing an N-terminal region of AmphDI and a C-terminal region of PerDI. This work will assist efforts to generate glycorandomised amphoteronolides for drug discovery.
Sponsorship
Higher Education Authority
Science Foundation Ireland
Other Sponsorship
European Union
BBSRC
Type of Material
Journal Article
Publisher
Elsevier
Journal
Chemistry and Biology
Volume
17
Issue
2
Start Page
174
End Page
182
Copyright (Published Version)
2010 Elsevier
Keywords
  • CHEMBIO

DOI
10.1016/j.chembiol.2010.01.007
Language
English
Status of Item
Peer reviewed
This item is made available under a Creative Commons License
https://creativecommons.org/licenses/by-nc-nd/3.0/ie/
Owning collection
Biomolecular and Biomedical Science Research Collection
Scopus© citations
36
Acquisition Date
Feb 4, 2023
View Details
Views
1247
Acquisition Date
Feb 5, 2023
View Details
Downloads
328
Last Week
5
Last Month
33
Acquisition Date
Feb 5, 2023
View Details
google-scholar
University College Dublin Research Repository UCD
The Library, University College Dublin, Belfield, Dublin 4
Phone: +353 (0)1 716 7583
Fax: +353 (0)1 283 7667
Email: mailto:research.repository@ucd.ie
Guide: http://libguides.ucd.ie/rru

Built with DSpace-CRIS software - Extension maintained and optimized by 4Science

  • Cookie settings
  • Privacy policy
  • End User Agreement