ReviewCurrent drug metabolism2008
Arylamine N-acetyltransferases in mycobacteria.
Review in Current drug metabolism, 2008. 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Preparation of Lipophilic Derivatives ofACS omega · 2025Article
- Dynamic microfluidic single-cell screening identifies pheno-tuning compounds to potentiate tuberculosis therapy.Nature communications · 2024Article
- Combined enhancement of the propionyl-CoA metabolic pathway for efficient androstenedione production in Mycolicibacterium neoaurum.Microbial cell factories · 2022Article
- Using Isoniazid More Safely and More Effectively: The Time Is Now.American journal of respiratory and critical care medicine · 2021Article
- Antimycobacterial, Enzyme Inhibition, and Molecular Interaction Studies of Psoromic Acid inJournal of clinical medicine · 2018Article
- Cholesterol metabolism: a potential therapeutic target in Mycobacteria.British journal of pharmacology · 2017Review
- The Redox Cofactor FApplied and environmental microbiology · 2016Article
- A Mutasynthetic Library of Platensimycin and Platencin Analogues.Organic letters · 2016Article
- TB Summit 2014: prevention, diagnosis, and treatment of tuberculosis-a meeting report of a Euroscicon conference.Virulence · 2014Article
- Arylamine N-acetyltransferases: from drug metabolism and pharmacogenetics to drug discovery.British journal of pharmacology · 2014Review
- New approaches to target the mycolic acid biosynthesis pathway for the development of tuberculosis therapeutics.Current pharmaceutical design · 2014Review
- Arylamine N-acetyltransferases: a structural perspective.British journal of pharmacology · 2013Review
- Identification of the enzyme responsible for N-acetylation of norfloxacin by Microbacterium sp. Strain 4N2-2.Applied and environmental microbiology · 2013Article
- Article
- Pathway profiling in Mycobacterium tuberculosis: elucidation of cholesterol-derived catabolite and enzymes that catalyze its metabolism.The Journal of biological chemistry · 2011Article
- New N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF.The Journal of biological chemistry · 2011Article
- cAMP-regulated protein lysine acetylases in mycobacteria.The Journal of biological chemistry · 2010Article
- Insights into the phylogeny or arylamine N-acetyltransferases in fungi.Journal of molecular evolution · 2010Article
- Probing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active site.Protein & cell · 2010Article
- Identification of arylamine N-acetyltransferase inhibitors as an approach towards novel anti-tuberculars.Protein & cell · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Polymorphic Human arylamine N-acetyltransferase (NAT2) inactivates the anti-tubercular drug isoniazid by acetyltransfer from acetylCoA. There are active NAT proteins encoded by homologous genes in mycobacteria including M. tuberculosis, M. bovis BCG, M. smegmatis and M. marinum. Crystallographic structures of NATs from M. smegmatis and M. marinum, as native enzymes and with isoniazid bound share a similar fold with the first NAT structure, Salmonella typhimurium NAT. There are three approximately equal domains and an active site essential catalytic triad of cysteine, histidine and aspartate in the first two domains. An acetyl group from acetylCoA is transferred to cysteine and then to the acetyl acceptor e.g. isoniazid. M. marinum NAT binds CoA in a more open mode compared with CoA binding to human NAT2. The structure of mycobacterial NAT may promote its role in synthesis of cell wall lipids, identified through gene deletion studies. NAT protein is essential for survival of M. bovis BCG in macrophage as are the proteins encoded by other genes in the same gene cluster (hsaA-D). HsaA-D degrade cholesterol, essential for mycobacterial survival inside macrophage. Nat expression remains to be fully understood but is co-ordinated with hsaA-D and other stress response genes in mycobacteria. Amide synthase genes in the streptomyces are also nat homologues. The amide synthases are predicted to catalyse intramolecular amide bond formation and creation of cyclic molecules, e.g. geldanamycin. Lack of conservation of the CoA binding cleft residues of M. marinum NAT suggests the amide synthase reaction mechanism does not involve a soluble CoA intermediate during amide formation and ring closure.
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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.