The anaerobic degradation of l-serine and l-threonine in enterobacteria: networks of pathways and regulatory signals |
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Authors: | Gary Sawers |
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Affiliation: | (1) Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, UK e-mail: gary.sawers@bbsrc.ac.uk Tel. +44-1603-456900 ext. 2750; Fax + 44 1603 454970, GB |
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Abstract: | The mechanisms controlling the biosynthesis and degradation of l-serine and l-threonine are remarkably complex. Their metabolism forms a network of pathways linking several amino acids, central primary metabolites such as pyruvate, oxaloacetate and 3-phosphoglycerate, and C1 metabolism. Studies on the degradation of these amino acids in Escherichia coli have revealed the involvement of fascinating enzymes that utilise quite diverse catalytic mechanisms. Moreover, it is emerging that both environmental and metabolic signals have a major impact in controlling enzyme synthesis. This is exemplified by the anaerobically regulated tdc operon, which encodes a metabolic pathway for the degradation of serine and threonine. Studies on this pathway are beginning to provide insights into how an organism adapts its genetic makeup to meet the physiological demands of the cell. Received: 30 August 1998 / Accepted: 9 October 1998 |
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Keywords: | l-Serine l-threonine Anaerobiosis Pyridoxal 5′ -phosphate enzymes Iron-sulfur enzymes Glycyl radical enzymes Metabolism |
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