Associated Papers
Type I fatty acid synthase trapped in the octanoyl-bound state.
Rittner A et al.
Protein Science : a Publication of the Protein Society, 2020
31811668 (PubMed )
Supplement: PRO-29-589-s001.pdf
Catalytic residues are shared between two pseudosubunits of the dehydratase domain of the animal fatty acid synthase.
Pasta S et al.
Chemistry & Biology, 2007
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.
Rangan VS et al.
The Journal of Biological Chemistry, 1998
The malonyl/acetyltransferase and beta-ketoacyl synthase domains of the animal fatty acid synthase can cooperate with the acyl carrier protein domain of either subunit.
Joshi AK et al.
Biochemistry, 1998
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