Evidence map›Paper›PMID 40595587›Full record

ArticleNature communications2025

A generalized platform for artificial intelligence-powered autonomous enzyme engineering.

Nilmani Singh, Stephan Lane, Tianhao Yu, Jingxia Lu, Adrianna Ramos, Haiyang Cui, Huimin Zhao

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Applications and limitations of AI tools in enzyme design.Protein science : a publication of the Protein Society · 2026
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Protein foundation models: a comprehensive survey.Science China. Life sciences · 2026
    Review
  12. Review
  13. Article
  14. Review
  15. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

7 authors.

Nilmani Singh *Carl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA.ORCID http://orcid.org/0000-0002-3684-7022
Stephan Lane *Carl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA.ORCID http://orcid.org/0000-0001-8041-1579
Tianhao YuCarl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA.
Jingxia LuCarl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA.ORCID http://orcid.org/0000-0002-8635-8753
Adrianna RamosCarl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA.
Haiyang CuiNSF Molecule Maker Lab Institute, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA.ORCID http://orcid.org/0000-0001-8360-0447
Huimin ZhaoCarl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA. zhao5@illinois.edu.ORCID http://orcid.org/0000-0002-9069-6739

Funding

U.S. Department of Energy (DOE) DE-SC0018420
6 · The paper itself

Abstract

Proteins are the molecular machines of life with numerous applications in energy, health, and sustainability. However, engineering proteins with desired functions for practical applications remains slow, expensive, and specialist-dependent. Here we report a generally applicable platform for autonomous enzyme engineering that integrates machine learning and large language models with biofoundry automation to eliminate the need for human intervention, judgement, and domain expertise. Requiring only an input protein sequence and a quantifiable way to measure fitness, this automated platform can be applied to engineer a wide array of proteins. As a proof of concept, we engineer Arabidopsis thaliana halide methyltransferase (AtHMT) for a 90-fold improvement in substrate preference and 16-fold improvement in ethyltransferase activity, along with developing a Yersinia mollaretii phytase (YmPhytase) variant with 26-fold improvement in activity at neutral pH. This is accomplished in four rounds over 4 weeks, while requiring construction and characterization of fewer than 500 variants for each enzyme. This platform for autonomous experimentation paves the way for rapid advancements across diverse industries, from medicine and biotechnology to renewable energy and sustainable chemistry.

Indexed as

Artificial IntelligenceProtein Engineering6-PhytaseArabidopsisArabidopsis ProteinsBacterial ProteinsHydrogen-Ion ConcentrationMachine LearningMethyltransferasesSubstrate SpecificityYersinia6-PhytaseArabidopsis ProteinsBacterial ProteinsMethyltransferases

Identifiers

PMID40595587
PMCPMC12215622

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.