Evidence map›Paper›PMID 36759590›Full record

ArticleNature methods2023

EnzymeML: seamless data flow and modeling of enzymatic data.

Simone Lauterbach, Hannah Dienhart, Jan Range, Stephan Malzacher, Jan-Dirk Spöring, Dörte Rother, Maria Filipa Pinto, Pedro Martins, Colton E Lagerman, Andreas S Bommarius and 13 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature methods, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Predicting Functional Diversity Within Enzyme Families: A Practical Perspective.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. A Guide to Bayesian Optimization in Bioprocess Engineering.Biotechnology and bioengineering · 2026
    Review
  3. Advances in Machine Learning Models for Predicting Enzyme Kinetic Parameters.Journal of chemical information and modeling · 2026
    Review
  4. Article
  5. Best Practices for Machine Learning-Assisted Protein Engineering.Journal of chemical information and modeling · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Activity assays for flavoprotein oxidases: an overview.Applied microbiology and biotechnology · 2025
    Review
  11. Review
  12. Review
  13. Enzyme Databases in the Era of Omics and Artificial Intelligence.International journal of molecular sciences · 2023
    Review
  14. Review
  15. Article
  16. Article
  17. 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

23 authors.

Simone LauterbachInstitute of Biochemistry and Technical Biochemistry, University of Stuttgart, Stuttgart, Germany.
Hannah DienhartInstitute of Biochemistry and Technical Biochemistry, University of Stuttgart, Stuttgart, Germany.
Jan RangeInstitute of Biochemistry and Technical Biochemistry, University of Stuttgart, Stuttgart, Germany.
Stephan MalzacherInstitute of Bio- and Geosciences 1, Forschungszentrum Jülich, Jülich, Germany.
Jan-Dirk SpöringInstitute of Bio- and Geosciences 1, Forschungszentrum Jülich, Jülich, Germany.ORCID http://orcid.org/0000-0002-5656-3537
Dörte RotherInstitute of Bio- and Geosciences 1, Forschungszentrum Jülich, Jülich, Germany.
Maria Filipa Pintoi3S, Instituto de Investigação e Inovação em Saúde da Universidade do Porto, University of Porto, Porto, Portugal.ORCID http://orcid.org/0000-0002-6337-3459
Pedro Martinsi3S, Instituto de Investigação e Inovação em Saúde da Universidade do Porto, University of Porto, Porto, Portugal.
Colton E LagermanSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, USA.
Andreas S BommariusSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, USA.ORCID http://orcid.org/0000-0003-4658-1675
Amalie Vang HøstDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, Kgs Lyngby, Denmark.
John M WoodleyDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, Kgs Lyngby, Denmark.ORCID http://orcid.org/0000-0002-7976-2483
Sandile NgubaneDepartment of Biotechnology and Food Science, Durban University of Technology, Durban, South Africa.ORCID http://orcid.org/0000-0003-4930-4526
Tukayi KudangaDepartment of Biotechnology and Food Science, Durban University of Technology, Durban, South Africa.ORCID http://orcid.org/0000-0003-0958-9846
Frank T BergmannBioQUANT/COS, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-5553-4702
Johann M RohwerDepartment of Biochemistry, Stellenbosch University, Stellenbosch, South Africa.ORCID http://orcid.org/0000-0001-6288-8904
Dorothea IglezakisInformation and Communication Center, University of Stuttgart, Stuttgart, Germany.ORCID http://orcid.org/0000-0002-8524-0569
Andreas WeidemannHeidelberg Institute for Theoretical Studies, Heidelberg, Germany.
Ulrike WittigHeidelberg Institute for Theoretical Studies, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-9077-5664
Carsten KettnerBeilstein-Institut, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-8697-6842
Neil SwainstonInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
Santiago SchnellDepartment of Biological Sciences and Department of Applied and Computational Mathematics and Statistics, University of Notre Dame, Notre Dame, IN, USA.ORCID http://orcid.org/0000-0002-9477-3914
Jürgen PleissInstitute of Biochemistry and Technical Biochemistry, University of Stuttgart, Stuttgart, Germany. Juergen.Pleiss@itb.uni-stuttgart.de.ORCID http://orcid.org/0000-0003-1045-8202

Funding

U.S. Department of Health & Human Services | U.S. Food and Drug Administration (U.S. Food & Drug Administration) Grant U01FD006484
6 · The paper itself

Abstract

The design of biocatalytic reaction systems is highly complex owing to the dependency of the estimated kinetic parameters on the enzyme, the reaction conditions, and the modeling method. Consequently, reproducibility of enzymatic experiments and reusability of enzymatic data are challenging. We developed the XML-based markup language EnzymeML to enable storage and exchange of enzymatic data such as reaction conditions, the time course of the substrate and the product, kinetic parameters and the kinetic model, thus making enzymatic data findable, accessible, interoperable and reusable (FAIR). The feasibility and usefulness of the EnzymeML toolbox is demonstrated in six scenarios, for which data and metadata of different enzymatic reactions are collected and analyzed. EnzymeML serves as a seamless communication channel between experimental platforms, electronic lab notebooks, tools for modeling of enzyme kinetics, publication platforms and enzymatic reaction databases. EnzymeML is open and transparent, and invites the community to contribute. All documents and codes are freely available at https://enzymeml.org .

Indexed as

Data ManagementMetadataDatabases, FactualKineticsReproducibility of Results

Identifiers

What OpenQuestion holds

Textmetadata
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.