ArticleBiochemistry2014
Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases.
Article in Biochemistry, 2014. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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, 34 citations in OpenAlex.
- Combining photo-CIDNP and long-lived spin states enables high-contrast detection of weak protein-ligand interactions.Physical chemistry chemical physics : PCCP · 2026Article
- Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.Biomolecular NMR assignments · 2025Article
- Distinct and Dynamic Changes in the Temporal Profiles of Neurotransmitters inPharmaceuticals (Basel, Switzerland) · 2023Article
- Melatonin biosynthesis pathways in nature and its production in engineered microorganisms.Synthetic and systems biotechnology · 2022Review
- Article
- 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
- Bm-iAANAT3: Expression and characterization of a novel arylalkylamine N-acyltransferase from Bombyx mori.Archives of biochemistry and biophysics · 2019Article
- Editorial: Aromatic Amino Acid Metabolism.Frontiers in molecular biosciences · 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 ArylalkylamineFrontiers in molecular biosciences · 2018Review
- Insect ArylalkylamineBiochemistry & molecular biology journal · 2018Article
- 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
- Probing the chemical mechanism and critical regulatory amino acid residues of Drosophila melanogaster arylalkylamine N-acyltransferase like 2.Insect biochemistry and molecular biology · 2015Article
- Mechanistic analysis of ghrelin-O-acyltransferase using substrate analogs.Bioorganic chemistry · 2015Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Arylalkylamine N-acetyltransferase (AANAT) catalyzes the penultimate step in the biosynthesis of melatonin and other N-acetylarylalkylamides from the corresponding arylalkylamine and acetyl-CoA. The N-acetylation of arylalkylamines is a critical step in Drosophila melanogaster for the inactivation of the bioactive amines and the sclerotization of the cuticle. Two AANAT variants (AANATA and AANATB) have been identified in D. melanogaster, in which AANATA differs from AANATB by the truncation of 35 amino acids from the N-terminus. We have expressed and purified both D. melanogaster AANAT variants (AANATA and AANATB) in Escherichia coli and used the purified enzymes to demonstrate that this N-terminal truncation does not affect the activity of the enzyme. Subsequent characterization of the kinetic and chemical mechanism of AANATA identified an ordered sequential mechanism, with acetyl-CoA binding first, followed by tyramine. We used a combination of pH-activity profiling and site-directed mutagenesis to study prospective residues believed to function in AANATA catalysis. These data led to an assignment of Glu-47 as the general base in catalysis with an apparent pKa of 7.0. Using the data generated for the kinetic mechanism, structure-function relationships, pH-rate profiles, and site-directed mutagenesis, we propose a chemical mechanism for AANATA.
Indexed as
Identifiers
What OpenQuestion holds
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.