ArticleThe Journal of biological chemistry2011
A complex lipoate utilization pathway in Listeria monocytogenes.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Adaptive metabolic strategies of intracellular bacterial pathogens.Frontiers in microbiology · 2026Review
- Fatty acid synthesis and utilization in gram-positive bacteria: insights fromMicrobiology and molecular biology reviews : MMBR · 2025Review
- Lipoic acid attachment to proteins: stimulating new developments.Microbiology and molecular biology reviews : MMBR · 2024Review
- Substrate Analogues Entering the Lipoic Acid Salvage Pathway via Lipoate-Protein Ligase 2 Interfere withACS infectious diseases · 2024Article
- A Chemical Proteomic Strategy Reveals Inhibitors of Lipoate Salvage in Bacteria and Parasites.Angewandte Chemie (International ed. in English) · 2023Article
- Identification of a novel lipoic acid biosynthesis pathway reveals the complex evolution of lipoate assembly in prokaryotes.PLoS biology · 2023Article
- Egress of Listeria monocytogenes from Mesenteric Lymph Nodes Depends on Intracellular Replication and Cell-to-Cell Spread.Infection and immunity · 2023Article
- A Novel Lipoate-Protein Ligase, Mhp-LplJ, Is Required for Lipoic Acid Metabolism inFrontiers in microbiology · 2020Article
- Functional Identification and Structural Analysis of a New Lipoate Protein Ligase inFrontiers in cellular and infection microbiology · 2020Article
- Dynamic Relay of Protein-Bound Lipoic Acid in Staphylococcus aureus.Journal of bacteriology · 2019Article
- Metabolism of the Gram-Positive Bacterial PathogenMicrobiology spectrum · 2019Review
- Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Increased flexibility in the use of exogenous lipoic acid by Staphylococcus aureus.Molecular microbiology · 2018Article
- Development and retention of a primordial moonlighting pathway of protein modification in the absence of selection presents a puzzle.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A novel lipoate attachment enzyme is shared by Plasmodium and Chlamydia species.Molecular microbiology · 2017Article
- Listeria monocytogenes cytosolic metabolism promotes replication, survival, and evasion of innate immunity.Cellular microbiology · 2017Review
- Staphylococcus aureus Tissue Infection During Sepsis Is Supported by Differential Use of Bacterial or Host-Derived Lipoic Acid.PLoS pathogens · 2016Article
- Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic Pathway.Microbiology and molecular biology reviews : MMBR · 2016Review
- The Streptomyces coelicolor lipoate-protein ligase is a circularly permuted version of the Escherichia coli enzyme composed of discrete interacting domains.The Journal of biological chemistry · 2015Article
- The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis.Yeast (Chichester, England) · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.