Mitochondrial beta-ketoacyl-acyl carrier protein synthase

Mitochondrial beta-ketoacyl-acyl carrier protein synthase is a key enzyme of the mitochondrial type II fatty acid synthesis pathway, catalyzing the condensation of an acyl group attached to an acyl carrier protein (ACP) with malonyl-ACP to form a β-ketoacyl-ACP and CO₂[4][5]. This enzyme, also known as OXSM or mtKAS, plays an essential role in the elongation of fatty acid chains within the mitochondrial matrix, supporting both energy metabolism and the synthesis of lipoic acid, an essential cofactor for mitochondrial enzyme complexes[1][3]. Its activity is critical in maintaining mitochondrial function; deficiencies alter lipid metabolism and can have broad metabolic consequences[1][3]. Several antibiotics and investigational compounds (cerulenin, C75, thiolactomycin, and platensimycin) selectively inhibit this class of enzymes by covalently or non-covalently binding to its active site, disrupting fatty acid chain elongation[5][6]. The enzyme is classified under EC 2.3.1.180. If plant or prokaryotic systems are intended, note that the same enzymatic function occurs in those organisms but may be encoded by different gene names and with slightly varying substrate specificity[2][4]. If you need species-specific details or human gene/protein identifiers, please clarify.

Other names

3-Oxoacyl-[acyl-carrier-protein] synthaseOXSMβ-ketoacyl-[acyl carrier protein] synthaseβ-Ketoacyl-ACP synthasemtKAS

Inhibition of the Claisen condensation step of fatty acid synthesis via binding to the active site of the synthase[5][6]