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Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships.

Ursula Gerike·David W Hough·Nicholas J Russell·Michael L Dyall-Smith·Michael J Danson
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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 and also possess 2-methylcitrate synthase activity. The data are discussed with respect to the structure, function and evolution of citrate synthase and 2-methylcitrate synthase.

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Bacterial ProteinsCitrate (si)-SynthaseEscherichia coliGenes, BacterialOxo-Acid-LyasesJournal ArticleResearch Support, Non-U.S. Gov't

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Ursula Gerike, David W Hough, Nicholas J Russell, Michael L Dyall-Smith, Michael J Danson. 1998. Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships.. https://doi.org/10.1099/00221287-144-4-929

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