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Structure and mechanism of oxalate decarboxylase: A novel Mn and oxygen dependent enzyme involved in pH stress response
Reference
C18140
Principal Investigator / Supervisor
Professor Stephen Bornemann
Co-Investigators /
Co-Supervisors
Professor David Lawson
Institution
John Innes Centre
Department
Biological Chemistry
Funding type
Research
Value (£)
166,868
Status
Completed
Type
Research Grant
Start date
17/02/2003
End date
16/02/2006
Duration
36 months
Abstract
Bacillus subtilis oxalate decarboxylase is a newly identified enzyme involved in pH stress responses that requires manganese and dioxygen for activity, despite the conversion of oxalate to carbon dioxide and formate involving no net redox change. The structure of this enzyme will be determined in different oxidation states and with oxalate and inhibitors bound using X-ray crystallography. Site specific mutants will be prepared and characterised in order to understand the role of amino acids of the active in substrate binding, proton donation, stablisation of radical intermediates and the determination of reaction specificity.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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