The lipoate synthase from Escherichia coli is an iron-sulfur protein.

Article Details

Citation
Copy to clipboard

Ollagnier-de Choudens S, Fontecave M

The lipoate synthase from Escherichia coli is an iron-sulfur protein.

FEBS Lett. 1999 Jun 18;453(1-2):25-8.

PubMed ID
10403368 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
Lipoic acidLipoyl synthase, mitochondrialProteinHumans
Unknown
Not AvailableDetails