BMS 358 (Purdie)
tel. 01334 463411
fax. 01334 462595
Enzymology involves the structural and functional characterisation of proteins either in the cell or in purified form. Techniques of kinetic analysis, spectroscopy, structural determination, inhibitor studies, and molecular biology are combined to investigate how enzymes work.
We study particularly membrane bound mitochondrial enzymes. For example, mitochondrial monoamine oxidases A and B (MAO A and MAO B) are ubiquitous homodimeric FAD-containin oxidases that catalyse the oxidation of biogenic amines. Both enzymes play a vital role in the regulation of neurotransmitter levels in brain below) complement mechanistic studies of purified MAO A and its mutants to characterise the active site and the catalytic mechanism of the enzyme to aid in drug design.
At the cellular level, investigating a family of homologous enzymes such as the carnitine
acyltransferases permits investigation of the molecular basis of regulation. Different
members of this family mediate fatty acid trafficking and influence pathways such as
ketogenesis, lipid synthesis and membrane repair (see scheme below). Current projects
include characterisation of the active sites of the acyltransferases by kinetic and mutagenic
techniques concurrent with crystallisation trials and, at a cellular level, a study of fluorescent
fusion proteins to investigate cellular trafficking.
Honorary Fellow, Hannah Research Institute, Ayr, Scotland
Visiting Professor, Graduate Programme, University of Catania (2002-2006)
Basic Research Grant Panel, Science and Innovation, Enterprise Ireland (2002-4).
Presenter and Co-ordinator for Athena Women in Science events (from 2000).
Participant, Contemporary Poetry, Contemporary Science, Wellcome Trust
(source: symbiosis database)