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Structure and Function of Oxalate Oxidase

Reference	BBS/E/J/41004095
Principal Investigator / Supervisor	Professor Stephen Bornemann
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	312,413
Status	Completed
Type	Institute Project
Start date	01/06/1997
End date	31/03/2000
Duration	34 months

Abstract

The level of expression of germin and other germin-like proteins in plants is known to change during the germination and development of cereal embryos, fungal infection of cereals and the exposure of salt-tolerant plants to salt stress. The germins from wheat and barley have been shown recently to exhibit oxalate oxidase activity and convert oxalate to carbon dioxide and hydrogen peroxide in the presence of dioxygen. The calcium ions that are liberated from insoluble calcium oxalate deposits and the hydrogen peroxide that is produced can act as second messengers. Hydrogen peroxide is also essential in the peroxidase-mediated lignification of plant cell walls. Since there is no evidence from spectroscopic measurements for a flavin cofactor it is likely that a metal ion is involved in catalysis. The mechanism of these biocatalysts will be studied at the atomic level using spectroscopic and rapid kinetic techniques using natural substrates and substrate analogues in conjunction with molecular biology and protein crystallography.

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	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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