Evidence map›Paper›PMID 41953217›Full record

ArticleACS catalysis2026

The Discovery of

Lukas Drexler, Cristina Duran, Sílvia Osuna, Reinhard Sterner

Abstract read
In one paragraph

Article in ACS catalysis, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Lukas DrexlerInstitute of Biophysics and Physical Biochemistry, Regensburg Center for Biochemistry, University of Regensburg, Regensburg D-93040, Germany.ORCID https://orcid.org/0000-0001-8193-3256
Cristina DuranInstitut de Química Computacional i Catàlisi(IQCC) and Departament de Química,Universitat de Girona, Girona 17003, Spain.
Sílvia OsunaInstitut de Química Computacional i Catàlisi(IQCC) and Departament de Química,Universitat de Girona, Girona 17003, Spain.ORCID https://orcid.org/0000-0003-3657-6469
Reinhard SternerInstitute of Biophysics and Physical Biochemistry, Regensburg Center for Biochemistry, University of Regensburg, Regensburg D-93040, Germany.ORCID https://orcid.org/0000-0001-8177-8460

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The widespread use of xenobiotics has driven the rapid emergence of microbial degradation pathways. A prominent example is enzymes involved in the catabolism of the herbicide atrazine, which have evolved within the last few decades. Recently, we provided evidence that the second enzyme of the atrazine biodegradation pathway, hydroxyatrazine ethylaminohydrolase (AtzB), has evolved from a progenitor enzyme of the amidohydrolase superfamily (AtzB-CQNN) with guanine deaminase (GuaD) activity. However, the catalytic efficiency for guanine hydrolysis by AtzB-CQNN is several orders of magnitude lower than that of prototypical GuaDs. In this study, we report a much higher catalytic efficiency of AtzB-CQNN for the hydrolysis of the guanine analogue

Indexed as

amidohydrolase superfamilyconformational heterogeneityenzyme catalysisenzyme evolutionN2,N2-dimethylguanine hydrolasepromiscuityshortest path map analysisxenobiotics

Identifiers

PMID41953217
PMCPMC13054789

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.