2uv8

In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.

Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase., Leibundgut M, Jenni S, Frick C, Ban N, Science. 2007 Apr 13;316(5822):288-90. PMID:17431182

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Categories: Fatty-acyl-CoA synthase | Saccharomyces cerevisiae | Ban, N. | Frick, C. | Jenni, S. | Leibundgut, M. | Acetyl transferase | Acyl carrier protein | Dehydratase | Enoyl reductase | Fatty acid biosynthesis | Fatty acid synthase | Fatty acid synthesis | Hydrolase | Ketoacyl reductase | Ketoacyl synthase | Lipid synthesis | Lyase | Malonyl/palmitoyl transferase | Multifunctional enzyme | Nad | Nadp | Oxidoreductase | Phosphopantetheine | Phosphorylation | Substrate shuttling | Transferase | Yeast