ReviewMicrobiology and molecular biology reviews : MMBR2013
Acyltransferases in bacteria.
Review in Microbiology and molecular biology reviews : MMBR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
71 citing papers in PubMed, 168 citations in OpenAlex.
- Structural lipid modifications associated with the persister state in Acinetobacter baumannii: LC-TIMS-TOF for collision cross section determination and focus on uncommon wax esters.Analytical and bioanalytical chemistry · 2026Article
- The evolutionary processes of bacterial aromatic polyketide ketosynthases.Genome biology · 2026Article
- Metabolic engineering of cereal lipids: from omega-3 fatty acids to wax esters and pheromones.Advanced biotechnology · 2026Review
- Alternative enzymatic pathways to penicillin antibiotics.Nature communications · 2026Article
- O-acyltransferase genes involved in the production of volatile sex pheromones inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Biosynthesis, characterisation and biocompatibility of a unique and elastomeric medium chain-length polyhydroxyalkanoates for kidney glomerular tissue engineering.Materials today. Bio · 2025Article
- Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.The Journal of biological chemistry · 2025Article
- The WSD-type wax ester synthase is widely conserved in streptophytes and crucial for floral organ formation under high humidity in land plants.Journal of plant research · 2025Article
- Synthetic Lipid Biology.Chemical reviews · 2025Review
- Microalgae and cyanobacteria as microbial substrate and their influence on the potential postbiotic capability of a bacterial probiotic.Microbial biotechnology · 2024Article
- Enzyme-like Acyl Transfer Catalysis in a Bifunctional Organic Cage.Journal of the American Chemical Society · 2024Article
- Comparative analysis of metabolic models of microbial communities reconstructed from automated tools and consensus approaches.NPJ systems biology and applications · 2024Article
- Acylation of glycerolipids in mycobacteria.Nature communications · 2023Article
- Exploring aRSC chemical biology · 2023Article
- Potential of Natural Phenolic Compounds as Antimicrobial Agents against Multidrug-ResistantMolecules (Basel, Switzerland) · 2023Article
- Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis.Nature communications · 2023Article
- Directed evolution of a wax ester synthase for production of fatty acid ethyl esters in Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2023Article
- Article
- Future Antimicrobials: Natural and Functionalized Phenolics.Molecules (Basel, Switzerland) · 2023Review
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Long-chain-length hydrophobic acyl residues play a vital role in a multitude of essential biological structures and processes. They build the inner hydrophobic layers of biological membranes, are converted to intracellular storage compounds, and are used to modify protein properties or function as membrane anchors, to name only a few functions. Acyl thioesters are transferred by acyltransferases or transacylases to a variety of different substrates or are polymerized to lipophilic storage compounds. Lipases represent another important enzyme class dealing with fatty acyl chains; however, they cannot be regarded as acyltransferases in the strict sense. This review provides a detailed survey of the wide spectrum of bacterial acyltransferases and compares different enzyme families in regard to their catalytic mechanisms. On the basis of their studied or assumed mechanisms, most of the acyl-transferring enzymes can be divided into two groups. The majority of enzymes discussed in this review employ a conserved acyltransferase motif with an invariant histidine residue, followed by an acidic amino acid residue, and their catalytic mechanism is characterized by a noncovalent transition state. In contrast to that, lipases rely on completely different mechanism which employs a catalytic triad and functions via the formation of covalent intermediates. This is, for example, similar to the mechanism which has been suggested for polyester synthases. Consequently, although the presented enzyme types neither share homology nor have a common three-dimensional structure, and although they deal with greatly varying molecule structures, this variety is not reflected in their mechanisms, all of which rely on a catalytically active histidine residue.
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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.