1955-13-1

Upstream product

• 300-30-1 thyroxine 
• 72-89-9 acetylcoenzyme A 
• 86154-71-4 3,5,3',5'-tetraiodo-thyronine methyl ester 
• 108-24-7 acetic anhydride 
• 93315-06-1 N-acetyl-3,5-diiodo-thyronine 
• 67843-98-5 N-acetyl-3,5,3',5'-tetraiodo-thyronine methyl ester 

Relevant academic research and scientific papers

Unexpected Acetylation of Endogenous Aliphatic Amines by Arylamine N-Acetyltransferase NAT2

N-Acetyltransferases play critical roles in the deactivation and clearance of xenobiotics, including clinical drugs. NAT2 has been classified as an arylamine N-acetyltransferase that mainly converts aromatic amines, hydroxylamines, and hydrazines. Herein, we demonstrate that the human arylamine N-acetyltransferase NAT2 also acetylates aliphatic endogenous amines. Metabolomic analysis and chemical synthesis revealed increased intracellular concentrations of mono- and diacetylated spermidine in human cell lines expressing the rapid compared to the slow acetylator NAT2 phenotype. The regioselective N8-acetylation of monoacetylated spermidine by NAT2 answers the long-standing question of the source of diacetylspermidine. We also identified selective acetylation of structurally diverse alkylamine-containing drugs by NAT2, which may contribute to variations in patient responses. The results demonstrate a previously unknown functionality and potential regulatory role for NAT2, and we suggest that this enzyme should be considered for re-classification.