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Updated: Jul 29, 2026

An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase
Published on: December 20, 2010
The lipoate synthase from Escherichia coli is an iron-sulfur protein
S Ollagnier-de Choudens1, M Fontecave
1Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DBMS-CB, CEA/CNRS/Université Joseph Fourier, Grenoble, France.
Abstract:
Lipoate synthase catalyzes the last step of the biosynthesis of lipoic acid in microorganisms and plants. The protein isolated from an overexpressing Escherichia coli strain was purified from inclusion bodies. Spectroscopic (UV-visible and electron paramagnetic resonance) properties of the reconstituted protein demonstrate the presence of a (2Fe-2S) center per protein. As observed in biotin synthase, these clusters are converted to (4Fe-4S) centers during reduction under anaerobic conditions. The possible involvement of the cluster in the insertion of sulfur atoms into the octanoic acid backbone is discussed.
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