Elsevier Description Serine acetyltransferase (SAT; EC 2.3.1.30) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of l-serine to form O-acetyl serine, in the first step of the l-cysteine biosynthetic pathway. Since this pathway is selectively present in a few parasitic protists and absent in mammals, it represents a reasonable target to develop new chemotherapeutics. Entamoeba histolytica apparently possesses three SAT isotypes (EhSAT1-3) showing 48–73% mutual identity, a calculated molecular mass of 34.4–37.7kDa, and an isoelectric point of 5.70–6.63. To better understand the role of individual SAT isotypes, we determined kinetic and inhibitory parameters of...