ReviewBiochimica et biophysica acta2015
Moonlighting O-acetylserine sulfhydrylase: New functions for an old protein.
Review in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 47 citations in OpenAlex.
- Comparative proteomics reveal striking differences in biofilm formation and virulence potential ofJournal of bacteriology · 2026Article
- Serine Acetyltransferase fromInternational journal of molecular sciences · 2026Article
- The Curious Case of CysE: Diversity and Distribution of Serine Acetyltransferases in Bacteria.Proteins · 2026Article
- Distinct contributions of O-acetylserine sulfhydrylases to cysteine biosynthesis in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2026Article
- Article
- Structure-Functional Examination of Cysteine Synthase A (CysK) fromInternational journal of molecular sciences · 2025Article
- Benzotriazole derivatives as alternateiScience · 2025Article
- Identification of Cysteine Metabolism Regulator (CymR)-Derived Pentapeptides as Nanomolar Inhibitors ofACS infectious diseases · 2025Article
- Combatting antimicrobial resistance via the cysteine biosynthesis pathway in bacterial pathogens.Bioscience reports · 2022Review
- Review
- Brucella ovis Cysteine Biosynthesis Contributes to Peroxide Stress Survival and Fitness in the Intracellular Niche.Infection and immunity · 2021Article
- Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action.International journal of molecular sciences · 2019Article
- Nitrogen sourcing during viral infection of marine cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Review
- Characterization of the O-acetylserine(thiol)lyase gene family in Solanum lycopersicum L.Plant molecular biology · 2019Article
- Genetic, metabolomic and transcriptomic analyses of the de novo L-cysteine biosynthetic pathway in the enteric protozoan parasite Entamoeba histolytica.Scientific reports · 2017Article
- Activation of an anti-bacterial toxin by the biosynthetic enzyme CysK: mechanism of binding, interaction specificity and competition with cysteine synthase.Scientific reports · 2017Article
- Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex.FEBS letters · 2017Article
- Can't you hear me knocking: contact-dependent competition and cooperation in bacteria.Emerging topics in life sciences · 2017Article
- Unraveling the essential role of CysK in CDI toxin activation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
O-acetylserine sulfhydrylase A (CysK) is the pyridoxal 5'-phosphate-dependent enzyme that catalyzes the final reaction of cysteine biosynthesis in bacteria. CysK was initially identified in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This "cysteine synthase" complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Remarkably, the CysK/CysE binding interaction is conserved in most bacterial and plant systems. For the past 40years, CysK was thought to function exclusively in cysteine biosynthesis, but recent studies have revealed a repertoire of additional "moonlighting" activities for this enzyme. CysK and its paralogs influence transcription in both Gram-positive bacteria and the nematode Caenorhabditis elegans. CysK also activates an antibacterial nuclease toxin produced by uropathogenic Escherichia coli. Intriguingly, each moonlighting activity requires a binding partner that invariably mimics the C-terminus of CysE to interact with the CysK active site. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications.
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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.