ReviewMicrobiology and molecular biology reviews : MMBR2016
Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic Pathway.
Review in Microbiology and molecular biology reviews : MMBR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 152 citations in OpenAlex.
- Staphylococcus aureus adapts to the host nutritional environment by coordinating the activity of central metabolic enzymes.PLoS pathogens · 2026Article
- Complex interplay of riboregulatory mechanisms at theJournal of bacteriology · 2026Article
- MLL3/4 methyltransferases regulate the differentiation of pluripotent stem cells through coordinating glycolysis and mitochondrial respiration.bioRxiv : the preprint server for biology · 2026Article
- Targeting multiple genetic defects of mitochondrial diseases with a single bacterial lipoate protein ligase.Science advances · 2025Article
- Amplified copper ion interference and immunomodulation using self-thermophoretic nanomotors to treat refractory implant-associated biofilm infections.Nature communications · 2025Article
- Protein lipoylation in cancer: metabolic reprogramming and therapeutic potential.Cell death discovery · 2025Review
- Two putativeMicrobiology (Reading, England) · 2025Article
- Staphylococcus aureus exploits lipoic acid salvage to combat host oxidative stress.Cell reports · 2025Article
- Fatty acid synthesis and utilization in gram-positive bacteria: insights fromMicrobiology and molecular biology reviews : MMBR · 2025Review
- A globular protein exhibits rare phase behavior and forms chemically regulated orthogonal condensates in cells.Nature communications · 2025Article
- Defining the necessity of the lipoic acid synthasemicroPublication biology · 2025Article
- Article
- Metabolic capabilities are highly conserved among human nasal-associatedbioRxiv : the preprint server for biology · 2024Article
- A Multi-Target Pharmacological Correction of a LipoyltransferaseAntioxidants (Basel, Switzerland) · 2024Article
- Adaptive Evolution Signatures inMicroorganisms · 2024Article
- 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
- DecipheringmSystems · 2024Article
- Ultrasound-activated piezo-hot carriers trigger tandem catalysis coordinating cuproptosis-like bacterial death against implant infections.Nature communications · 2024Article
- Evolution at the Origins of Life?Life (Basel, Switzerland) · 2024Review
21 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although the structure of lipoic acid and its role in bacterial metabolism were clear over 50 years ago, it is only in the past decade that the pathways of biosynthesis of this universally conserved cofactor have become understood. Unlike most cofactors, lipoic acid must be covalently bound to its cognate enzyme proteins (the 2-oxoacid dehydrogenases and the glycine cleavage system) in order to function in central metabolism. Indeed, the cofactor is assembled on its cognate proteins rather than being assembled and subsequently attached as in the typical pathway, like that of biotin attachment. The first lipoate biosynthetic pathway determined was that of Escherichia coli, which utilizes two enzymes to form the active lipoylated protein from a fatty acid biosynthetic intermediate. Recently, a more complex pathway requiring four proteins was discovered in Bacillus subtilis, which is probably an evolutionary relic. This pathway requires the H protein of the glycine cleavage system of single-carbon metabolism to form active (lipoyl) 2-oxoacid dehydrogenases. The bacterial pathways inform the lipoate pathways of eukaryotic organisms. Plants use the E. coli pathway, whereas mammals and fungi probably use the B. subtilis pathway. The lipoate metabolism enzymes (except those of sulfur insertion) are members of PFAM family PF03099 (the cofactor transferase family). Although these enzymes share some sequence similarity, they catalyze three markedly distinct enzyme reactions, making the usual assignment of function based on alignments prone to frequent mistaken annotations. This state of affairs has possibly clouded the interpretation of one of the disorders of human lipoate metabolism.
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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.