NDLI: Structure and function of animal fatty acid synthase

Content Provider	Springer Nature Link
Author	Chirala, Subrahmanyam S. Wakil, Salih J.
Copyright Year	2004
Abstract	Fatty acid synthase (FAS; EC 2.3.1.85) of animal tissues is a complex multifunctional enzyme consisting of two identical monomers. The FAS monomer (∼270 kDa) contains six catalytic activities and from the N-terminus the order is β-ketoacyl synthase (KS), acetyl/malonyl transacylase (AT/MT), β-hydroxyacyl dehydratase (DH), enoyl reductase (ER), β-ketoacyl reductase (KR), acyl carrier protein (ACP), and thioesterase (TE). Although the FAS monomer contains all the activities needed for palmitate synthesis, only the dimer form of the synthase is functional. Both the biochemical analyses and the small-angle neutron-scattering analysis determined that in the dimer form of the enzyme the monomers are arranged in a head-to-tail manner generating two centers for palmitate synthesis. Further, these analyses also suggested that the component activities of the monomer are organized in three domains. Domain I contains KS, AT/MT, and DH, domain II contains ER, KR, and ACP, and domain III contains TE. Approximately one fourth of the monomer protein located between domains I and II contains no catalytic activities and is called the interdomain/core region. This region plays an important role in the dimer formation. Electron cryomicrographic analyses of FAS revealed a quaternary structure at approximately 19 Å resolution, containing two monomers (180×130×75 Å) that are separated by about 19 Å, and arranged in an antiparallel fashion, which is consistent with biochemical and neutron-scattering data. The monomers are connected at the middle by a hinge generating two clefts that may be the two active centers of fatty acid synthesis. Normal mode analysis predicted that the intersubunit hinge region and the intrasubunit hinge located between domains II and III are highly flexible. Analysis of FAS particle images by using a simultaneous multiple model single particle refinement method confirmed that FAS structure exists in various conformational states. Attempts to get higher resolution of the structure are under way.
Starting Page	1045
Ending Page	1053
Page Count	9
File Format	PDF
ISSN	00244201
Journal	Lipids
Volume Number	39
Issue Number	11
e-ISSN	15589307
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-01-01
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Lipidology Neurochemistry Medical Biochemistry Nutrition Medicinal Chemistry Microbial Genetics and Genomics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Organic Chemistry Biochemistry

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