Evidence map›Paper›PMID 26526101›Full record

ArticleChemistry & biology2015

Probing the Substrate Specificity and Protein-Protein Interactions of the E. coli Fatty Acid Dehydratase, FabA.

Kara Finzel, Chi Nguyen, David R Jackson, Aarushi Gupta, Shiou-Chuan Tsai, Michael D Burkart

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemistry & biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Control of Unsaturation inBiochemistry · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Interfacial plasticity facilitates high reaction rate ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Structural and dynamical rationale for fatty acid unsaturation inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Review
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Kara FinzelDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0358, USA.
Chi NguyenDepartments of Molecular Biology and Biochemistry, Chemistry and Pharmaceutical Sciences, University of California, Irvine, Irvine, CA 92697-1450, USA.
David R JacksonDepartments of Molecular Biology and Biochemistry, Chemistry and Pharmaceutical Sciences, University of California, Irvine, Irvine, CA 92697-1450, USA.
Aarushi GuptaDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0358, USA.
Shiou-Chuan TsaiDepartments of Molecular Biology and Biochemistry, Chemistry and Pharmaceutical Sciences, University of California, Irvine, Irvine, CA 92697-1450, USA. Electronic address: sctsai@uci.edu.
Michael D BurkartDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0358, USA. Electronic address: mburkart@ucsd.edu.
University of California, Irvine · USUniversity of California San Diego · US

Funding

Protein-Protein Interactions in Natural Product BiosynthesisR01GM095970 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BURKART, MICHAEL D. · 2012 to 2025
$5.9M
The Molecular Basis of Regio-Specificity in Fungal Polyketide SynthaseR01GM100305 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI BURKART, MICHAEL D., TSAI, SHIOU-CHUAN · 2012 to 2015
$1.6M
NIGMS NIH HHS GM095970NIGMS NIH HHS GM100305NIGMS NIH HHS R01 GM095970NIGMS NIH HHS R01 GM100305
6 · The paper itself

Abstract

Microbial fatty acid biosynthetic enzymes are important targets for areas as diverse as antibiotic development to biofuel production. Elucidating the molecular basis of chain length control during fatty acid biosynthesis is crucial for the understanding of regulatory processes of this fundamental metabolic pathway. In Escherichia coli, the acyl carrier protein (AcpP) plays a central role by sequestering and shuttling the growing acyl chain between fatty acid biosynthetic enzymes. FabA, a β-hydroxyacyl-AcpP dehydratase, is an important enzyme in controlling fatty acid chain length and saturation levels. FabA-AcpP interactions are transient in nature and thus difficult to visualize. In this study, four mechanistic crosslinking probes mimicking varying acyl chain lengths were synthesized to systematically probe for modified chain length specificity of 14 FabA mutants. These studies provide evidence for the AcpP-interacting "positive patch," FabA mutations that alter substrate specificity, and the roles that the FabA "gating residues" play in chain length control.

Indexed as

Acyl Carrier ProteinBinding SitesCross-Linking ReagentsEscherichia coliFatty Acid Synthase, Type IIHydro-LyasesMolecular Dynamics SimulationMolecular ProbesMutagenesisProtein Interaction Domains and MotifsProtein Structure, TertiaryRecombinant ProteinsSubstrate Specificity3-hydroxyacyl-(acyl-carrier-protein) dehydrataseAcyl Carrier ProteinCross-Linking ReagentsFatty Acid Synthase, Type IIHydro-LyasesMolecular ProbesRecombinant Proteins

Identifiers

PMID26526101
PMCPMC4656083
OpenAlexW1929246000

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.