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Mechanism of CMP-Neu5Ac hydroxylase
Reference
BCI06184
Principal Investigator / Supervisor
Professor Timothy Bugg
Co-Investigators /
Co-Supervisors
Institution
University of Southampton
Department
Sch of Chemistry
Funding type
Research
Value (£)
42,159
Status
Completed
Type
Research Grant
Start date
17/01/1997
End date
17/02/1998
Duration
13 months
Abstract
The objectives of the proposed research are to elucidate the stereochemistry and mechanism of CMP-N-acetylneuraminic acid hydroxylase, a non-haem iron (II) dependent oxygenase enzyme involved in the biosynthesis of sialic acid-containing glycoconjugates. A series of N-acyl-neuraminic acid analogues will be synthesised from D-glycosamine using the enzyme N-acetylneuraminic acid aldolase. The stereochemistry of the enzymatic reaction will be deduced using stereospecifically labelled N-propionyl-analogues, and the intermediacy of enolate vs. radical intermediates will be assessed using isotope exchange and cyclopropyl radical traps.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Biological Chemistry Initiative (BCI) [1995]
Funding Scheme
X – not Funded via a specific Funding Scheme
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