ArticleProstaglandins, leukotrienes, and essential fatty acids2018
Bm-iAANAT and its potential role in fatty acid amide biosynthesis in Bombyx mori.
Article in Prostaglandins, leukotrienes, and essential fatty acids, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Engineering of Corynebacterium glutamicum for biosynthesis of the pharmaceutically active N-acetyltyramine: establishing and optimizing de novo production.Journal of biological engineering · 2026Article
- Plasma metabolomic profiling reveals lipid biomarkers for early detection of exercise-induced myocardial ischemia.Medicine · 2026Article
- Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.Biomolecular NMR assignments · 2025Article
- Synthesis, Quantification, and Characterization of Fatty Acid Amides from In Vitro and In Vivo Sources.Molecules (Basel, Switzerland) · 2021Review
- The Biosynthesis and Metabolism of theFrontiers in molecular biosciences · 2021Review
- Identification of catalytically distinct arylalkylamine N-acetyltransferase splicoforms from Tribolium castaneum.Protein expression and purification · 2020Article
- An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase.Communications biology · 2020Article
- Knockdown of arylalkylamine N-acetyltransferase-like 2 in Drosophila melanogaster.Archives of insect biochemistry and physiology · 2019Article
- 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
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7 authors.
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Abstract
The purpose of this research is to unravel the substrate specificity and kinetic properties of an insect arylalkylamine N-acyltransferase from Bombyx mori (Bm-iAANAT) and to determine if this enzyme will catalyze the formation of long chain N-acylarylalkylamides in vitro. However, the determination of substrates and products for Bm-iAANAT in vitro is no guarantee that these same molecules are substrates and products for the enzyme in the organism. Therefore, RT-PCR was performed to detect the Bm-iAANAT transcripts and liquid chromatography quadrupole time-of-flight mass spectrometry (LC-QToF-MS) analysis was performed on purified lipid extracts from B. mori larvae (fourth instar, Bmi4) to determine if long chain fatty acid amides are produced in B. mori. Ultimately, we found that recombinant Bm-iAANAT will utilize long-chain acyl-CoA thioesters as substrates and identified Bm-iAANAT transcripts and long-chain fatty acid amides in Bmi4. Together, these data show Bm-iAANAT will catalyze the formation of long-chain N-acylarylalkylamides in vitro and provide evidence demonstrating that Bm-iAANAT has a role in fatty acid amide biosynthesis in B. mori, as well.
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