Evidence map›Paper›PMID 26867580›Full record

ArticleThe Journal of biological chemistry2016

Control of the Position of Oxygen Delivery in Soybean Lipoxygenase-1 by Amino Acid Side Chains within a Gas Migration Channel.

Lara Collazo, Judith P Klinman

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
  2. Review
  3. Article
  4. Elucidating the Role of OACS environmental Au · 2024
    Article
  5. Article
  6. Soybean (International journal of molecular sciences · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. EPR Spectroscopic Studies of Lipoxygenases.Chemistry, an Asian journal · 2020
    Review
  13. The Biosynthesis of Enzymatically Oxidized Lipids.Frontiers in endocrinology · 2020
    Review
  14. Moving Through Barriers in Science and Life.Annual review of biochemistry · 2019
    Article
  15. Article
  16. Fast Hydrogen Atom Abstraction by a Hydroxo Iron(III) Porphyrazine.Journal of the American Chemical Society · 2017
    Article
  17. Journal of the American Chemical Society · 2017
    Article
  18. Synthesis of Site-SpecificallyTetrahedron letters · 2016
    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

2 authors.

Lara CollazoFrom the Department of Molecular and Cell Biology, Department of Chemistry, and the California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, California 94720.
Judith P KlinmanFrom the Department of Molecular and Cell Biology, Department of Chemistry, and the California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, California 94720 klinman@berkeley.edu.

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
Toward a Comprehensive Model for Enzyme CatalysisR01GM025765 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 1985 to 2015
$7.1M
DOPAMINE MONOOXYGENASE--MOLECULAR MECHANISMSR37GM025765 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH POLLOCK · 1990 to 1999
–
NIGMS NIH HHS R01 GM025765NIGMS NIH HHS R35 GM118117NIGMS NIH HHS R37 GM025765
6 · The paper itself

Abstract

Understanding gas migration pathways is critical to unraveling structure-function relationships in enzymes that process gaseous substrates such as O2, H2, and N2 This work investigates the role of a defined pathway for O2 in regulating the peroxidation of linoleic acid by soybean lipoxygenase 1. Computational and mutagenesis studies provide strong support for a dominant delivery channel that shuttles molecular oxygen to a specific region of the active site, thereby ensuring the regio- and stereospecificity of product. Analysis of reaction kinetics and product distribution in channel mutants also reveals a plasticity to the gas migration pathway. The findings show that a single site mutation (I553W) limits oxygen accessibility to the active site, greatly increasing the fraction of substrate that reacts with oxygen free in solution. They also show how a neighboring site mutation (L496W) can result in a redirection of oxygen toward an alternate position of the substrate, changing the regio- and stereospecificity of peroxidation. The present data indicate that modest changes in a protein scaffold may modulate the access of small gaseous molecules to enzyme-bound substrates.

Indexed as

Mutation, MissenseAmino Acid SubstitutionGlycine maxLipoxygenaseOxygenSoybean ProteinsLipoxygenaseOxygenSoybean Proteinscatalysisenzyme mechanismenzyme mutationkineticslipoxygenaseoxygen channelprotein structureregio- and stereospecificity

Identifiers

PMID26867580
PMCPMC4861474

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.