Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase

Mycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis.

Mycolic acids consist of long-chain alpha-alkyl-beta-hydroxy fatty acids that are produced by successive rounds of elongation catalysed by a type II fatty acid synthase (FAS-II). A key feature in the elongation process is the condensation of a two-carbon unit from malonyl-acyl-carrier protein (ACP) to a growing acyl-ACP chain catalysed by a beta-ketoacyl-ACP synthase (Kas). In the present study...

The 3-hydroxyacyl-ACP dehydratase component of the plant mitochondrial fatty acid synthase system

Fatty acid synthetases from Euglena gracilis. Separation of component activities of the ACP-dependent fatty acid synthetase and partial purification of the beta-ketoacyl-ACP synthetase.

The component enzymes of the chloroplast-associated, acyl carrier protein (ACP)-dependent, fatty acid synthetase (FAS-11) from Euglena gracilis have been independently examined by gel filtration chromatography of crude extracts from photoautotrophic cells. The acetyl coenzyme A:ACP transacylase, malonyl CoA:ACP transacylase, and /3-ketoacyl-ACP reductase activities were clearly resolved with a...

Protein interactions of fatty acid synthase II.

We have used a yeast two-hybrid approach to detect direct protein interactions between fatty acid synthase components. Enoyl-acyl carrier protein (ACP) reductase was found to interact with stearoyl-ACP desaturase and acyl-ACP thioesterase, but none of these proteins interacted with ACP in the yeast nucleus.

Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.

In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein (ACP) synthases catalyze chain elongation by the addition of two-carbon units derived from malonyl-ACP to an acyl group bound to either ACP or CoA. The crystal structure of beta-ketoacyl synthase II from Escherichia coli has been determined with the multiple isomorphous replacement method and refined at 2.4 A resolution....