Fatty acid synthase dimers containing catalytically active beta-ketoacyl synthase or malonyl/acetyltransferase domains in only one subunit can support fatty acid synthesis at the acyl carrier protein domains of both subunits.

Abstract excerpt

A double-tagging, dual affinity chromatographic procedure, which permits isolation of dimers independently mutated in each subunit, has been exploited to probe the functional topology of the animal fatty acid synthase. Dimers were engineered in which the chain-terminating thioesterase reaction wa...

Topics

• 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase
• Acetyl Coenzyme A
• Acyl Carrier Protein
• Acyltransferases
• Catalytic Domain
• Dimerization
• Fatty Acid Synthases
• Fatty Acids
• Malonyl Coenzyme A
• Mutation