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Structure of the mitochondrial β‐ketoacyl‐[acyl carrier protein] synthase from Arabidopsis and its role in fatty acid synthesis
Author(s) -
Olsen Johan G.,
Rasmussen Anne V.,
von Wettstein-Knowles Penny,
Henriksen Anette
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.007
Subject(s) - fatty acid synthase , acyl carrier protein , atp synthase , biochemistry , fatty acid , enzyme , arabidopsis thaliana , fatty acid synthesis , arabidopsis , mitochondrion , stereochemistry , plastid , chemistry , biology , biosynthesis , gene , chloroplast , mutant
Mitochondrial fatty acid synthesis is catalyzed by a dissociated fatty acid synthase similar to those of plant plastids and bacteria. The crystal structure of a mitochondrial β‐ketoacyl‐[acyl carrier protein] synthase (mtKAS), namely that from Arabidopsis thaliana , has been determined for the first time. This enzyme accomplishes the vital condensation steps in constructing fatty acid carbon skeletons. The product profile of mtKAS is unusual in that C 8 and C 14–16 fatty acyl chains predominate. An enzyme architecture that likely is the basis for the observed bimodal profile of mtKAS products can be derived from the shape of the acyl binding pocket.