ArticleProceedings of the National Academy of Sciences of the United States of America2012
Evolution of insect arylalkylamine N-acetyltransferases: structural evidence from the yellow fever mosquito, Aedes aegypti.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 55 citations in OpenAlex.
- Insect-specific aldehyde synthase governs cuticle strength: a selective insecticide target.Science advances · 2026Article
- A Testis-Specific Aralkylamine N-Acetyltransferase Regulates Dimorphic Sperm Function and Male Fertility in Moths.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.Biomolecular NMR assignments · 2025Article
- Mapping Gene Expression in Whole Larval Brains ofMethods and protocols · 2025Article
- A Structurally Diverse Compound Screening Library to Identify Substrates for Diamine, Polyamine, and Related Acetyltransferases.ACS omega · 2024Article
- Evolutionary formation of melatonin and vitamin D in early life forms: insects take centre stage.Biological reviews of the Cambridge Philosophical Society · 2024Review
- Evolutionary Genomics Reveals Multiple Functions of ArylalkylamineFrontiers in genetics · 2022Review
- Gcn5-RelatedFrontiers in molecular biosciences · 2021Article
- Identification of catalytically distinct arylalkylamine N-acetyltransferase splicoforms from Tribolium castaneum.Protein expression and purification · 2020Article
- Anopheles metabolic proteins in malaria transmission, prevention and control: a review.Parasites & vectors · 2020Review
- An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase.Communications biology · 2020Article
- Who Rules the Cell? An Epi-Tale of Histone, DNA, RNA, and the Metabolic Deep State.Frontiers in plant science · 2020Review
- RNA interference-mediated knockdown of 3, 4-dihydroxyphenylacetaldehyde synthase affects larval development and adult survival in the mosquito Aedes aegypti.Parasites & vectors · 2019Article
- Editorial: Aromatic Amino Acid Metabolism.Frontiers in molecular biosciences · 2019Article
- Bm-iAANAT3: Expression and characterization of a novel arylalkylamine N-acyltransferase from Bombyx mori.Archives of biochemistry and biophysics · 2019Article
- Bm-iAANAT and its potential role in fatty acid amide biosynthesis in Bombyx mori.Prostaglandins, leukotrienes, and essential fatty acids · 2018Article
- Eis, a novel family of arylalkylamine N-acetyltransferase (EC 2.3.1.87).Scientific reports · 2018Article
- Insect ArylalkylamineBiochemistry & molecular biology journal · 2018Article
- Identification of aaNAT5b as a spermine N-acetyltransferase in the mosquito, Aedes aegypti.PloS one · 2018Article
- Insect ArylalkylamineFrontiers in molecular biosciences · 2018Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Arylalkylamine N-acetyltransferase (aaNAT) catalyzes the transacetylation from acetyl-CoA to arylalkylamines. aaNATs are involved in sclerotization and neurotransmitter inactivation in insects. Phyletic distribution analysis confirms three clusters of aaNAT-like sequences in insects: typical insect aaNAT, polyamine NAT-like aaNAT, and mosquito unique putative aaNAT (paaNAT). Here we studied three proteins: aaNAT2, aaNAT5b, and paaNAT7, each from a different cluster. aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as the previously identified arylalkylamines. aaNAT5b, a protein from polyamine NAT -like aaNAT cluster, uses hydrazine and histamine as substrates. The crystal structure of aaNAT2 was determined using single-wavelength anomalous dispersion methods, and that of native aaNAT2, aaNAT5b and paaNAT7 was detected using molecular replacement techniques. All three aaNAT structures have a common fold core of GCN5-related N-acetyltransferase superfamily proteins, along with a unique structural feature: helix/helices between β3 and β4 strands. Our data provide a start toward a more comprehensive understanding of the structure-function relationship and physiology of aaNATs from the mosquito Aedes aegypti and serve as a reference for studying the aaNAT family of proteins from other insect species. The structures of three different types of aaNATs may provide targets for designing insecticides for use in mosquito control.
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