Evidence map›Paper›PMID 39300819›Full record

ArticleAngewandte Chemie (International ed. in English)2024

Indole N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions.

Jiasong Li, Ran Duan, Ephrahime S Traore, Romie C Nguyen, Ian Davis, Wendell P Griffth, Douglas C Goodwin, Andrzej A Jarzecki, Aimin Liu

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Catalase-peroxidase (KatG): a potential frontier in tuberculosis drug development.Critical reviews in biochemistry and molecular biology · 2024
    Review
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

9 authors.

Jiasong LiDepartment of Chemistry, The University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX 78249, USA.ORCID 0000-0003-0341-2038
Ran DuanDepartment of Chemistry, The University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX 78249, USA.
Ephrahime S TraoreDepartment of Chemistry, The University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX 78249, USA.ORCID 0000-0001-6419-9248
Romie C NguyenDepartment of Chemistry, The University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX 78249, USA.ORCID 0000-0002-9450-2364
Ian DavisDepartment of Chemistry, The University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX 78249, USA.ORCID 0000-0002-1566-4972
Wendell P GriffthDepartment of Chemistry, The University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX 78249, USA.ORCID 0000-0003-2633-6103
Douglas C GoodwinDepartment of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA.
Andrzej A JarzeckiDepartment of Chemistry and Biochemistry, Brooklyn College, New York, NY 11210, USA.
Aimin LiuDepartment of Chemistry, The University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX 78249, USA.ORCID 0000-0002-4182-8176

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Thomas Michael Weiss · 2020 to 2026
$43.3M
Heme-dependent chemistry in tyrosine oxidation: Diversity Supplement on 5R01GM108988-08 for supporting Samuel MontoyaR01GM108988 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI LIU, AIMIN · 2014 to 2025
$4.2M
Protein-Derived Cofactor in Bifunctional Enzyme KatG from Mycobacterium tuberculosisR01GM152982 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI Aimin Liu · 2024 to 2026
$1.0M
Structure-Function Relationship study of HupZF31GM145187 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI TRAORE, EPHRAHIME · 2022 to 2024
$117k
Directorate for Biological Sciences MCB-1616059Directorate for Mathematical and Physical Sciences CHE-2204225NIGMS NIH HHS F31 GM145187NIGMS NIH HHS F31GM145187NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R01 GM108988NIGMS NIH HHS R01GM108988NIGMS NIH HHS R01 GM152982NIGMS NIH HHS R01GM152982Welch Foundation AX-2110-20220331
6 · The paper itself

Abstract

Bifunctional catalase-peroxidase (KatG) features a posttranslational methionine-tyrosine-tryptophan (MYW) crosslinked cofactor crucial for its catalase function, enabling pathogens to neutralize hydrogen peroxide during infection. We discovered the presence of indole nitrogen-linked hydroperoxyl adduct (MYW-OOH) in Mycobacterium tuberculosis KatG in the solution state under ambient conditions, suggesting its natural occurrence. By isolating predominantly MYW-OOH-containing KatG protein, we investigated the chemical stability and functional impact of MYW-OOH. We discovered that MYW-OOH inhibits catalase activity, presenting a unique temporary lock. Exposure to peroxide or increased temperature removes the hydroperoxyl adduct from the protein cofactor, converting MYW-OOH to MYW and restoring the detoxifying ability of the enzyme against hydrogen peroxide. Thus, the N-linked hydroperoxyl group is releasable. KatG with MYW-OOH represents a catalase dormant, but primed, state of the enzyme. These findings provide insight into chemical strategies targeting the bifunctional enzyme KatG in pathogens, highlighting the role of N-linked hydroperoxyl modifications in enzymatic function.

Indexed as

CatalaseIndolesMycobacterium tuberculosisBacterial ProteinsHydrogen PeroxidePeroxidesBacterial ProteinsCatalaseHydrogen PeroxideindoleIndoleskatG protein, Mycobacterium tuberculosisPeroxidesbacterial pathogenenzyme catalysishemeoxygenationprotein cofactor

Identifiers

PMID39300819
PMCPMC11686441

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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.