Thialysine N-epsilon-acetyltransferase (SAT2)

Thialysine N-epsilon-acetyltransferase (SAT2) is an enzyme that primarily acetylates the naturally occurring modified amino acid thialysine [S-(2-aminoethyl)-L-cysteine] at the ε-amino group, converting it to S-(2-acetylaminoethyl)-L-cysteine[1][2]. While it shares sequence similarity with spermidine/spermine N1-acetyltransferase 1 (SSAT1), SAT2 has extremely poor activity toward classical polyamine substrates and does not participate significantly in polyamine catabolism[1][2]. Its preferred substrate is thialysine, distinguishing it from SSAT1, which regulates polyamine homeostasis[1]. SAT2 is widely expressed but is not regulated by polyamine analogues and is considered part of the GNAT (GCN5-related N-acetyltransferase) family[2]. No strong links to major diseases have been established, and it is not the current target of any approved drugs or therapeutic strategies[2].

Other names

Spermidine/spermine N1-acetyltransferase family member 2SSAT2Diamine acetyltransferase 2Polyamine N-acetyltransferase 2Thialysine N-epsilon-acetyltransferaseDiamine N-acetyltransferase 2

Not established for clinical drugs; the enzyme acetylates thialysine, influencing modified amino acid and potentially brain ketimine metabolism[1]