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  • Title: The iron-sulfur cluster in the L-serine dehydratase TdcG from Escherichia coli is required for enzyme activity.
    Author: Burman JD, Harris RL, Hauton KA, Lawson DM, Sawers RG.
    Journal: FEBS Lett; 2004 Oct 22; 576(3):442-4. PubMed ID: 15498577.
    Abstract:
    The anaerobically inducible L-serine dehydratase, TdcG, from Escherichia coli was characterized. Based on UV-visible spectroscopy, iron and labile sulfide analyses, the homodimeric enzyme is proposed to have two oxygen-labile [4Fe-4S]2+ clusters. Anaerobically isolated dimeric TdcG had a kcat of 544 s(-1) and an apparent KM for L-serine of 4.8 mM. L-threonine did not act as a substrate for the enzyme. Exposure of the active enzyme to air resulted in disappearance of the broad absorption band at 400-420 nm, indicating a loss of the [4Fe-4S]2+ cluster. A concomitant loss of dehydratase activity was demonstrated, indicating that integrity of the [4Fe-4S]2+ cluster is essential for enzyme activity.
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