AI Article Synopsis
- Lipoic acid metabolism is well-understood in E. coli but is more complex in other bacteria, like Listeria monocytogenes, which uses two lipoate-protein ligases.
- Scavenging lipoic acid involves ligation and a lipoyl relay pathway where an amidotransferase helps transfer lipoyl groups to enzyme complexes needing them.
- New evidence suggests a lipoamidase activity that enhances the ability of lipoate-protein ligase to utilize lipoyl peptides, forming a three-enzyme pathway for lipoic acid scavenging observed in many bacteria from the Firmicutes phylum.
Article Abstract
Although a complete pathway of lipoic acid metabolism has been established in Escherichia coli, lipoic acid metabolism in other bacteria is more complex and incompletely understood. Listeria monocytogenes has been shown to utilize two lipoate-protein ligases for lipoic acid scavenging, whereas only one of the ligases can function in utilization of host-derived lipoic acid-modified peptides. We report that lipoic acid scavenging requires not only ligation of lipoic acid but also a lipoyl relay pathway in which an amidotransferase transfers lipoyl groups to the enzyme complexes that require the cofactor for activity. In addition, we provide evidence for a new lipoamidase activity that could allow utilization of lipoyl peptides by lipoate-protein ligase. These data support a model of an expanded, three-enzyme pathway for lipoic acid scavenging that seems widespread in the Firmicutes phylum of bacteria.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3173067 | PMC |
| http://dx.doi.org/10.1074/jbc.M111.273607 | DOI Listing |
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