ArticleJournal of the American Chemical Society2011
Enzymatic deamination of the epigenetic base N-6-methyladenine.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 29 citations in OpenAlex.
- Growth ofBiomolecules · 2026Article
- The Discovery ofACS catalysis · 2026Article
- The C-terminal structure of the N6-methyladenosine deaminase YerA and its role in deamination.The Biochemical journal · 2025Article
- Means, mechanisms and consequences of adenine methylation in DNA.Nature reviews. Genetics · 2022Review
- Review
- N6-methyladenine: A Rare and Dynamic DNA Mark.Advances in experimental medicine and biology · 2022Article
- Enzymatic deamination of the epigenetic nucleoside N6-methyladenosine regulates gene expression.Nucleic acids research · 2021Article
- DNA Methylation on N6-Adenine Regulates the Hyphal Development during Dimorphism in the Early-Diverging FungusJournal of fungi (Basel, Switzerland) · 2021Article
- DNA NPlants (Basel, Switzerland) · 2020Review
- N6-Methyladenine: A Conserved and Dynamic DNA Mark.Advances in experimental medicine and biology · 2016Review
- Application of DNA adductomics to soil bacterium Sphingobium sp. strain KK22.MicrobiologyOpen · 2015Article
- Leveraging structure for enzyme function prediction: methods, opportunities, and challenges.Trends in biochemical sciences · 2014Review
- Prediction of substrates for glutathione transferases by covalent docking.Journal of chemical information and modeling · 2014Article
- Structure-guided discovery of new deaminase enzymes.Journal of the American Chemical Society · 2013Article
- Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes.Biochemistry · 2013Article
- Theoretical study on the binding mechanism between N6-methyladenine and natural DNA bases.Journal of molecular modeling · 2013Article
- Assignment of pterin deaminase activity to an enzyme of unknown function guided by homology modeling and docking.Journal of the American Chemical Society · 2013Article
- Structure-based function discovery of an enzyme for the hydrolysis of phosphorylated sugar lactones.Biochemistry · 2012Article
- Statistical potential for modeling and ranking of protein-ligand interactions.Journal of chemical information and modeling · 2011Article
- The Enzyme Function Initiative.Biochemistry · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Two enzymes of unknown function from the amidohydrolase superfamily were discovered to catalyze the deamination of N-6-methyladenine to hypoxanthine and methyl amine. The methylation of adenine in bacterial DNA is a common modification for the protection of host DNA against restriction endonucleases. The enzyme from Bacillus halodurans, Bh0637, catalyzes the deamination of N-6-methyladenine with a k(cat) of 185 s(-1) and a k(cat)/K(m) of 2.5 × 10(6) M(-1) s(-1). Bh0637 catalyzes the deamination of N-6-methyladenine 2 orders of magnitude faster than adenine. A comparative model of Bh0637 was computed using the three-dimensional structure of Atu4426 (PDB code: 3NQB) as a structural template and computational docking was used to rationalize the preferential utilization of N-6-methyladenine over adenine. This is the first identification of an N-6-methyladenine deaminase (6-MAD).
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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.