Identification of an arylalkylamine N-acyltransferase from Drosophila melanogaster that catalyzes the formation of long-chain N-acylserotonins
| Autor: | Santiago Rodriquez Opsina, David J. Merkler, Ryan L. Anderson, Daniel R. Dempsey, Kristen A. Jeffries, Anne-Marie Carpenter |
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| Jazyk: | angličtina |
| Předmět: |
Cell signaling
Serotonin N-acylserotonin Biophysics Biochemistry Gene Expression Regulation Enzymologic Article Thorax-abdomen 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Structural Biology Steady-state kinetics Genetics Animals N-acyldopamine RNA Messenger Arylalkylamine N-acyltransferase Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Colocalization Fatty acid Arylalkylamine N-acetyltransferase Cell Biology biology.organism_classification 3. Good health Drosophila melanogaster chemistry Acyltransferases Organ Specificity Acyltransferase Arylalkylamine Biocatalysis Adenosine triphosphate 030217 neurology & neurosurgery |
| Zdroj: | FEBS Letters. (4):594-599 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2013.12.027 |
| Popis: | Arylalkylamine N-acyltransferase-like 22The authors recommend the change of arylalkylamine N-acetyltransferase to arylalkylamine N-acyltransferase due to the discovery of acyl-CoA substrates longer than C2 (acetyl).2 (AANATL2) from Drosophila melanogaster was expressed and shown to catalyze the formation of long-chain N-acylserotonins and N-acydopamines. Subsequent identification of endogenous amounts of N-acylserotonins and colocalization of these fatty acid amides and AANATL2 transcripts gives supporting evidence that AANATL2 has a role in the biosynthetic formation of these important cell signalling lipids. |
| Databáze: | OpenAIRE |
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