Format

Send to

Choose Destination
J Biol Chem. 2011 Sep 9;286(36):31447-56. doi: 10.1074/jbc.M111.273607. Epub 2011 Jul 18.

A complex lipoate utilization pathway in Listeria monocytogenes.

Author information

1
Department of Microbiology, University of Illinois, Urbana, Illinois 61801, USA.

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.

PMID:
21768091
PMCID:
PMC3173067
DOI:
10.1074/jbc.M111.273607
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center