A fatty acid amide is precisely as the name suggests: A fatty acid (CHn-COOH), in which the hydroxyl group of the carboxylic acid is displaced by an amine functional group from a biogenic amine (R-NH2), ultimately forming an amide bond. Furthermore, these fatty acid amides can be composed of a variety of different acyl chain lengths donated by the fatty acid and a myriad of different biogenic amines. Thus, these molecules can be subdivided in a number of different ways including the separation of short chain (acetyl to heptanoyl) and long chain (palmitoyl to arachidonoyl) and also based off the biogenic amine type. The long chain fatty acid amides quickly gained the interest of the scientific community through the discovery of anandamide (N-arachidonoylethanolamide), which was found to be the endogenous ligand for the cannabinoid receptor-1 (CB1) found in the mammalian brain. This particular neural molecule is an N-acylethanolamide, which is one specific classification of long chain fatty acid amide. However, there exist other types of long chain fatty acid amides including the N-acylglycines, primary fatty acid amides (PFAMs) and N-acylarylalkylamides. Yet, despite the type of fatty acid amide, it has been shown many of these types of molecules are synthesized using a type of N-acyltransferase. These N-acyltransferases are believed to be members of the GCN5-related superfamily of N-acyltransferases (GNAT), which share the feature of being able to accept acyl-CoA thioester substrates. This dissertation will discuss and demonstrate the extraction of all types of the aforementioned classifications of long chain fatty acid amides but will have a particular focus on the N-acylarylalkylamides. Elucidating more about the biosynthetic pathways and metabolic routes of the long chain fatty acid amides could lead to the development of potential therapeutics and pest control agents. We have determined Drosophila melanogaster arylalkylamine N-acyltransferase like 2 is responsible for the in vivo biosynthesis of N-acyldopamines. We have also demonstrated Bombyx mori is another suitable model systems for the study of long chain fatty acid amides, as three insect arylalkylamine N-acyltrasnferase from Bombyx mori (Bm-iAANAT) were found to share some homology in primary sequence (25-29%) to AAANTL2 in Drosophila melanogaster. We show herein that one of these enzymes is able to catalyze the formation of long chain N-acylarylalkylamides in vivo. The change in the transcription of these enzymes was tracked to try and understand if these enzymes serve a focused purpose in the physiological development of the insect. If it is found one of these Bm-iAANAT are crucial for growth, it may elucidate a general function of the enzyme, which may be able to inhibit growth of specific insects that are known pests, while not targeting endangered insects like Apis melliferra (honey bee). Understanding this would help in the eventual creation of targeted insecticides on specific insect pests Furthermore, a novel panel of fatty acid amides was characterized and quantified in extracts from this organism via LC-QToF-MS, ultimately showing it is very possible the Bm-iAANATs are performing this catalysis in vivo.