ATase

ATase is an abbreviation used in scientific literature with several distinct meanings depending on the field. Most commonly, ATase refers to acetyltransferases, a broad class of enzymes that catalyze the transfer of acetyl groups from acetyl-CoA to acceptor substrates, including proteins, small molecules, and drugs. This group includes members such as GNAT family enzymes that act on amines, histone acetyltransferases that modify chromatin, and arylalkylamine N-acetyltransferases involved in melatonin synthesis. ATases play central roles in metabolism, gene regulation, drug resistance, and secondary metabolism in microorganisms.

Less commonly, ATase has been used in older literature as an abbreviation for aminotransferases, enzymes that transfer amino groups during amino acid metabolism. In modern practice, specific terms such as aspartate transaminase (AST) and alanine transaminase (ALT) are preferred. The nonstandard use of ATase for aminotransferases can lead to confusion, so context should be consulted.

Mechanism and structure: Acetyltransferases typically operate via a transfer mechanism that moves the acetyl group from acetyl-CoA to a substrate such as an amine, thiol, or another nucleophile. They often rely on conserved motifs and adopt diverse structural folds, ranging from small GNAT domains to larger, multi-domain histone acetyltransferases. This diversity underpins their broad substrate specificity and regulatory functions.

Clinical and research relevance: Serum levels of AST and ALT are commonly used clinical markers for liver health, illustrating how transaminases intersect with medical diagnostics. In research and drug development, acetyltransferase activity is studied to understand metabolism and to design inhibitors that counteract antibiotic resistance or modulate epigenetic states. ATase remains a flexible shorthand that requires careful context to avoid ambiguity.