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Chemical mechanism and 3-D active site of methylaspartate ammonia-lyase
Reference
BCI05857
Principal Investigator / Supervisor
Professor David Gani
Co-Investigators /
Co-Supervisors
Institution
University of Birmingham
Department
School of Chemistry
Funding type
Research
Value (£)
149,663
Status
Completed
Type
Research Grant
Start date
01/12/1996
End date
01/02/2000
Duration
38 months
Abstract
Previous work on methylaspartase in our own laboratory and work on partially homologous enzymes in others' laboratories has reached the stage where a full 3-D mechanistic picture of the methylaspartase reaction is timely and feasible. The current application seeks to draw previous kinetic, kinetic isotope, substrate specificity, SAR, chemical model and amino acid sequence data into a 3-D context using the fact that the metal ion binding regions of methylaspartase are similar to more simple enzymes. The scientific objectives are to completely characterise a dehydroalanine residue and determine the exact role of the metal ions. Chemical synthesis, physical organic chemistry, site-directed mutagenesis and NMR will play major roles in these studies.
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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