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Structural and mechanistic studies on anthocyanidin synthase and related oxygenases

Reference	B18672
Principal Investigator / Supervisor	Professor Christopher Joseph Schofield
Co-Investigators / Co-Supervisors	Dr K Harlos
Institution	University of Oxford
Department	Oxford Chemistry
Funding type	Research
Value (£)	175,468
Status	Completed
Type	Research Grant
Start date	23/08/2003
End date	22/08/2006
Duration	36 months

Abstract

Anthocyanidin synthase (ANS) is an Fe(II) dependent oxygenase catalysing the penultimate biosynthetic step of the important anthocyanidin group of flavonoids. Recent studies imply the principal in vitro product of ANS catalysed oxidation of its natural substrate, leuco anthocyanidin, are not anthocyanidins, but cis- dihydroflavanols. Solution of the ANS crystal structure enables dynamic studies and other studies to define its nascent products/mechanism and the role of ascorbate in oxygenase catalysis. The proposed in vivo involvement of ANS in a multi- enzyme complex in which its selectively is altered to produce anthocyanidins will be tested. The work is of general interest in respect of the studies on ascorbate and pathway channelling.

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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