ArticleArchives of biochemistry and biophysics2013
Alternative substrates selective for S-adenosylmethionine synthetases from pathogenic bacteria.
Article in Archives of biochemistry and biophysics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Engineering of Methionine Adenosyltransferase Reveals Key Roles of Electrostatic Interactions in Enhanced Catalytic Activity.Applied biochemistry and biotechnology · 2024Article
- Abietic Acid as a Novel Agent against Ocular Biofilms: An In Vitro and Preliminary In Vivo Investigation.International journal of molecular sciences · 2024Article
- Bacterial Biofilm Inhibition: A Focused Review on Recent Therapeutic Strategies for Combating the Biofilm Mediated Infections.Frontiers in microbiology · 2021Review
- Structure of a critical metabolic enzyme: S-adenosylmethionine synthetase from Cryptosporidium parvum.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Complementation of a metK-deficient E. coli strain with heterologous AdoMet synthetase genes.Microbiology (Reading, England) · 2017Article
- AdoMet analog synthesis and utilization: current state of the art.Current opinion in biotechnology · 2016Review
- Elaboration of a fragment library hit produces potent and selective aspartate semialdehyde dehydrogenase inhibitors.Bioorganic & medicinal chemistry · 2015Article
- A surprising range of modified-methionyl S-adenosylmethionine analogues support bacterial growth.Microbiology (Reading, England) · 2015Article
- A sensitive mass spectrum assay to characterize engineered methionine adenosyltransferases with S-alkyl methionine analogues as substrates.Analytical biochemistry · 2014Article
- Producing proficient methyl donors from alternative substrates of S-adenosylmethionine synthetase.Biochemistry · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
S-adenosyl-l-methionine (AdoMet) synthetase catalyzes the production of AdoMet, the major biological methyl donor and source of methylene, amino, ribosyl, and aminopropyl groups in the metabolism of all known organism. In addition to these essential functions, AdoMet can also serve as the precursor for two different families of quorum sensing molecules that trigger virulence in Gram-negative human pathogenic bacteria. The enzyme responsible for AdoMet biosynthesis has been cloned, expressed and purified from several of these infectious bacteria. AdoMet synthetase (MAT) from Neisseria meningitidis shows similar kinetic parameters to the previously characterized Escherichia coli enzyme, while the Pseudomonas aeruginosa enzyme has a decreased catalytic efficiency for its MgATP substrate. In contrast, the more distantly related MAT from Campylobacter jejuni has an altered quaternary structure and possesses a higher catalytic turnover than the more closely related family members. Methionine analogs have been examined to delineate the substrate specificity of these enzyme forms, and several alternative substrates have been identified with the potential to block quorum sensing while still serving as precursors for essential methyl donation and radical generation reactions.
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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.