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Structure and function of animal fatty acid synthase

Overview of attention for article published in Lipids, November 2004
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • Good Attention Score compared to outputs of the same age (73rd percentile)
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

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2 patents
wikipedia
23 Wikipedia pages

Citations

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154 Dimensions

Readers on

mendeley
159 Mendeley
Title
Structure and function of animal fatty acid synthase
Published in
Lipids, November 2004
DOI 10.1007/s11745-004-1329-9
Pubmed ID
Authors

Subrahmanyam S. Chirala, Salih J. Wakil

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 (approximately 270 kDa) contains six catalytic activities and from the N-terminus the order is beta-ketoacyl synthase (KS), acetyl/malonyl transacylase (AT/MT), beta-hydroxyacyl dehydratase (DH), enoyl reductase (ER), beta-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 A resolution, containing two monomers (180 x 130 x 75 A) that are separated by about 19 A, 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.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 159 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 <1%
China 1 <1%
Unknown 157 99%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 37 23%
Student > Bachelor 25 16%
Student > Master 24 15%
Researcher 11 7%
Student > Doctoral Student 8 5%
Other 21 13%
Unknown 33 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 49 31%
Agricultural and Biological Sciences 34 21%
Chemistry 18 11%
Medicine and Dentistry 6 4%
Pharmacology, Toxicology and Pharmaceutical Science 4 3%
Other 12 8%
Unknown 36 23%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 6. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 27 November 2023.
All research outputs
#4,808,622
of 23,221,875 outputs
Outputs from Lipids
#272
of 1,910 outputs
Outputs of similar age
#10,419
of 62,929 outputs
Outputs of similar age from Lipids
#5
of 14 outputs
Altmetric has tracked 23,221,875 research outputs across all sources so far. Compared to these this one has done well and is in the 76th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 1,910 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.9. This one has gotten more attention than average, scoring higher than 73% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 62,929 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 73% of its contemporaries.
We're also able to compare this research output to 14 others from the same source and published within six weeks on either side of this one. This one is in the 35th percentile – i.e., 35% of its contemporaries scored the same or lower than it.