Award details

Structure and mechanism of oxalate decarboxylase: a novel MN and oxygen dependent enzyme involved in PH stress response

Reference	BBS/E/J/0000A103
Principal Investigator / Supervisor	Professor Stephen Bornemann
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	38,544
Status	Completed
Type	Institute Project
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 - Plant & Microbial Sciences (PMS)
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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