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Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK
Department of Biological Sciences, Wye College, University of London, Wye, Kent TN25 5AH, UK
Department of Microbiology and Immunology, University of Melbourne, Parkville, Victoria 3052, Australia
ABSTRACT
Following the complete sequencing of the Escherichia coli genome, it has been shown that the proposed second citrate synthase of this organism, recently described by the authors, is in fact a 2-methylcitrate synthase that possesses citrate synthase activity as a minor component. Whereas the hexameric citrate synthase is constitutively produced, the 2-methylcitrate synthase is induced during growth on propionate, and the catabolism of propionate to succinate and pyruvate via 2-methylcitrate is proposed. The citrate synthases of the psychrotolerant eubacterium DS2-3R, and of the thermophilic archaea Thermoplasma acidophilum and Pyrococcus furiosus, are approximately 40% identical in sequence to the Escherichia coli 2-methylcitrate synthase andalso possess 2-methylcitrate synthase activity. The data are discussed with respect tothe structure, function and evolution of citrate synthase and 2-methylcitrate synthase.
*Author for correspondence: Michael J. Danson. Tel: + 44 1225 826509. Fax:. +44 1225 826779 e-mail: M.J.Danson@bath.ac.uk
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