Beta-ketoacyl-acyl carrier protein synthase II (KASII (also known as FabF))

Beta-ketoacyl-acyl carrier protein synthase II is a prokaryotic enzyme (EC 2.3.1.179) critical to the elongation phase of fatty acid biosynthesis. It catalyzes the addition of two-carbon units derived from malonyl-ACP to acyl-ACP chains via a Claisen condensation reaction. In Escherichia coli and other bacteria, KASII (FabF) is specifically involved in the conversion of palmitoleic acid (C16:1) to cis-vaccenic acid (C18:1) and plays a vital role in adapting membrane fluidity under temperature shifts. The enzyme is a homodimer, with each subunit featuring a mixed beta-sheet and associated alpha helices. KASII is not present in humans but is essential for bacterial viability, making it an attractive target for novel antibiotics. Its inhibition can disrupt bacterial cell membrane integrity and growth[1][2][3][5]. Caveat: The disease roles and drug information relate primarily to its role in bacterial pathogens (e.g., Mycobacterium tuberculosis) and not to direct human disease states. Structure and substrate specificity may vary between organisms.

Other names

KASIIKAS IIFabF3-oxoacyl-acyl carrier protein synthase IBeta-ketoacyl-ACP synthase II(Z)-hexadec-11-enoyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating)

Inhibition of fatty acid elongation (by blocking the condensation of malonyl-ACP and acyl-ACP substrates); Claisen condensation reaction inhibition[2][5]