Arylalkylamine N-acyltransferase, Dopamine, Fatty acid amide biosynthesis, Serotonin
Digital Object Identifier (DOI)
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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Citation / Publisher Attribution
Prostaglandins, Leukotrienes and Essential Fatty Acids, v. 135, p. 10-17
This article is the post-print author version.Final version available at: https://doi.org/10.1016/j.plefa.2018.06.001
Scholar Commons Citation
Anderson, Ryan L.; Battistini, Matthew R.; Wallis, Dylan J.; Shoji, Christopher; O'Flynn, Brian G.; Dillashaw, John E.; and Merkler, David J, "Bm-iAANAT and its Potential Role in Fatty Acid Amide Biosynthesis in Bombyx mori" (2018). Chemistry Faculty Publications. 63.