ArticleThe Biochemical journal2012
Crystal structure of the dopamine N-acetyltransferase-acetyl-CoA complex provides insights into the catalytic mechanism.
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.Biomolecular NMR assignments · 2025Article
- Possible Neuropathology of Sleep Disturbance Linking to Alzheimer's Disease: Astrocytic and Microglial Roles.Frontiers in cellular neuroscience · 2022Review
- Structural characterization of a GNAT family acetyltransferase from Elizabethkingia anophelis bound to acetyl-CoA reveals a new dimeric interface.Scientific reports · 2021Article
- Gcn5-RelatedFrontiers in molecular biosciences · 2021Article
- Identification of catalytically distinct arylalkylamine N-acetyltransferase splicoforms from Tribolium castaneum.Protein expression and purification · 2020Article
- Article
- An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase.Communications biology · 2020Article
- Alternative catalytic residues in the active site of Esco acetyltransferases.Scientific reports · 2020Article
- Article
- Bm-iAANAT3: Expression and characterization of a novel arylalkylamine N-acyltransferase from Bombyx mori.Archives of biochemistry and biophysics · 2019Article
- Insect ArylalkylamineFrontiers in molecular biosciences · 2018Review
- Structural and Mechanistic Analysis of Drosophila melanogaster Agmatine N-Acetyltransferase, an Enzyme that Catalyzes the Formation of N-Acetylagmatine.Scientific reports · 2017Article
- Acetyl group coordinated progression through the catalytic cycle of an arylalkylamine N-acetyltransferase.PloS one · 2017Article
- Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).International journal of molecular sciences · 2016Review
- Probing the chemical mechanism and critical regulatory amino acid residues of Drosophila melanogaster arylalkylamine N-acyltransferase like 2.Insect biochemistry and molecular biology · 2015Article
- Article
- Structural basis for substrate-specific acetylation of Nα-acetyltransferase Ard1 from Sulfolobus solfataricus.Scientific reports · 2015Article
- Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases.Biochemistry · 2014Article
- Molecular characterization of a novel N-acetyltransferase from Chryseobacterium sp.Applied and environmental microbiology · 2014Article
- Three-dimensional structure of a Streptomyces sviceus GNAT acetyltransferase with similarity to the C-terminal domain of the human GH84 O-GlcNAcase.Acta crystallographica. Section D, Biological crystallography · 2014Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The daily cycle of melatonin biosynthesis in mammals is regulated by AANAT (arylalkylamine N-acetyltransferase; EC 2.3.1.87), making it an attractive target for therapeutic control of abnormal melatonin production in mood and sleep disorders. Drosophila melanogaster Dat (dopamine N-acetyltransferase) is an AANAT. Until the present study, no insect Dat structure had been solved, and, consequently, the structural basis for its acetyl-transfer activity was not well understood. We report in the present paper the high-resolution crystal structure for a D. melanogaster Dat-AcCoA (acetyl-CoA) complex obtained using one-edge (selenium) single-wavelength anomalous diffraction. A binding study using isothermal titration calorimetry suggested that the cofactor bound to Dat first before substrate. Examination of the complex structure and a substrate-docked model indicated that Dat contains a novel AANAT catalytic triad. Site-directed mutagenesis, kinetic studies and pH-rate profiles confirmed that Glu(47), Ser(182) and Ser(186) were critical for catalysis. Collectively, the results of the present study suggest that Dat possesses a specialized active site structure dedicated to a catalytic mechanism.
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