Evidence map›Paper›PMID 34725510›Full record

ArticleNature chemical biology2021

Biosynthesis of triacsin featuring an N-hydroxytriazene pharmacophore.

Antonio Del Rio Flores, Frederick F Twigg, Yongle Du, Wenlong Cai, Daniel Q Aguirre, Michio Sato, Moriel J Dror, Maanasa Narayanamoorthy, Jiaxin Geng, Nicholas A Zill and 2 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

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  8. Structural Basis for the Catalytic Mechanism of ATP-Dependent Diazotase CmaA6.Angewandte Chemie (International ed. in English) · 2025
    Article
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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

12 authors.

Antonio Del Rio Flores *Department of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.ORCID http://orcid.org/0000-0001-5893-3557
Frederick F Twigg *Department of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.ORCID http://orcid.org/0000-0003-4074-4218
Yongle DuDepartment of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.
Wenlong CaiDepartment of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.
Daniel Q AguirreDepartment of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.
Michio SatoDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.ORCID http://orcid.org/0000-0002-6026-8426
Moriel J DrorDepartment of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.
Maanasa NarayanamoorthyDepartment of Chemistry, University of California Berkeley, Berkeley, CA, United States.ORCID http://orcid.org/0000-0002-7418-2607
Jiaxin GengDepartment of Plant and Microbial Biology, University of California Berkeley, Berkeley, CA, United States.
Nicholas A ZillDepartment of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.
Rui ZhaiDepartment of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States.ORCID http://orcid.org/0000-0001-5032-9689
Wenjun ZhangDepartment of Chemical and Biomolecular Engineering, University of California Berkeley, Berkeley, CA, United States. wjzhang@berkeley.edu.ORCID http://orcid.org/0000-0001-9348-972X

Funding

In Situ Natural Product Labeling and ApplicationsDP2AT009148 · NCCIH · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZHANG, WENJUN · 2015 to 2020
$2.8M
Biosynthesis of unusual bio-orthogonal functionalities in natural productsR01GM136758 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZHANG, WENJUN · 2020 to 2023
$1.5M
NCCIH NIH HHS DP2 AT009148NIGMS NIH HHS R01 GM136758
6 · The paper itself

Abstract

Triacsins are an intriguing class of specialized metabolites possessing a conserved N-hydroxytriazene moiety not found in any other known natural products. Triacsins are notable as potent acyl-CoA synthetase inhibitors in lipid metabolism, yet their biosynthesis has remained elusive. Through extensive mutagenesis and biochemical studies, we here report all enzymes required to construct and install the N-hydroxytriazene pharmacophore of triacsins. Two distinct ATP-dependent enzymes were revealed to catalyze the two consecutive N-N bond formation reactions, including a glycine-utilizing, hydrazine-forming enzyme (Tri28) and a nitrite-utilizing, N-nitrosating enzyme (Tri17). This study paves the way for future mechanistic interrogation and biocatalytic application of enzymes for N-N bond formation.

Indexed as

BiocatalysisCoenzyme A LigasesEscherichia coliGlycineHydrazinesLipid MetabolismLipidsLong-Chain-Fatty-Acid-CoA LigaseNitritesStreptomyces aureofaciensTriazenesCoenzyme A LigasesGlycinehydrazineHydrazinesLipidsLong-Chain-Fatty-Acid-CoA LigaseNitritesTriazenes

Identifiers

PMID34725510
PMCPMC8605994

What OpenQuestion holds

Textmetadata
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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.