Function
Serine acetyltransferase (SAT) catalyzes the reaction converting serine to O-acetyl-serine using acetyl-CoA as a cofactor. This reaction is the first step in the synthesis of cysteine in bacteria and plants[1]. SAT is regulated by a feedback inhibition by ots end product - cysteine.
Structural highlights
The structure of the complex of SAT with its substrate serine suggest that and that . for (water molecules are shown as red spheres). Arg253 is important for the catalytic efficiency of SAT. Lys230 is required for the cofactor acetyl-CoA binding[2].
