Evidence map›Paper›PMID 40758891›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Structural basis for anaerobic alkane activation by a multisubunit glycyl radical enzyme.

Mary C Andorfer, Talya S Levitz, Jian Liu, Ankush Chakraborty, Devin T King-Roberts, Delight Nweneka, Christa N Imrich, Catherine L Drennan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. The structural basis of malodorant skatole formation by the glycyl radical enzyme indoleacetate decarboxylase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. 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

8 authors.

Mary C AndorferDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.
Talya S LevitzDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
Jian LiuDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.
Ankush ChakrabortyDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.
Devin T King-RobertsDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139.
Delight NwenekaDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
Christa N ImrichDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Catherine L DrennanDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.ORCID 0000-0001-5486-2755

Funding

PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
TRAINING GRANTS IN ENVIROMENTAL TOXICOLOGYT32ES007020 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ESSIGMANN, JOHN M · 1985 to 2024
$13.1M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Investigation and application of hydrocarbon-degrading enzymes using cryo-electron microscopy and directed evolutionR00GM145910 · NIGMS · MICHIGAN STATE UNIVERSITY · PI ANDORFER, MARY CATHERINE · 2023 to 2025
$855k
Taming radical enzymes through directed evolution and structural analysisF32GM129882 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ANDORFER, MARY CATHERINE · 2018 to 2021
$193k
Investigation and application of hydrocarbon-degrading enzymes using cryo-electron microscopy and directed evolutionK99GM145910 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ANDORFER, MARY CATHERINE · 2022 to 2023
$112k
HHMI (HHMI) CLD is an InvestigatorHHS | NIH | National Institute of Environmental Health Sciences (DEHS) T32ES007020HHS | NIH | National Institute of General Medical Sciences (NIGMS) F32GM129882HHS | NIH | National Institute of General Medical Sciences (NIGMS) K99/R00GM145910HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM126982HHS | NIH | National Institute of General Medical Sciences (NIGMS) T32GM007287NIEHS NIH HHS T32 ES007020NIGMS NIH HHS F32 GM129882NIGMS NIH HHS K99 GM145910NIGMS NIH HHS R00 GM145910NIGMS NIH HHS R35 GM126982NIGMS NIH HHS T32 GM007287NSF | NSF Graduate Research Fellowship Program (GRFP) 2017246757
6 · The paper itself

Abstract

X-succinate synthases (XSSs) are glycyl radical enzymes (GREs) that catalyze the addition of hydrocarbons to fumarate via radical chemistry, thereby activating them for microbial metabolism. To date, the only structurally characterized XSS is benzylsuccinate synthase (BSS), which functionalizes toluene. A distinct subclass of XSSs acts on saturated hydrocarbons, which possess much stronger C(sp

Indexed as

AlkanesAzoarcusBacterial ProteinsCarbon-Carbon LyasesAnaerobiosisCatalytic DomainCryoelectron MicroscopyModels, MolecularProtein SubunitsAlkanesBacterial Proteinsbenzylsuccinate synthaseCarbon-Carbon LyasesProtein Subunitsanaerobic hydrocarbon degradationC–H functionalizationenvironmental remediationfumarate additionX-succinate synthase

Identifiers

PMID40758891
PMCPMC12358834

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.