Evidence map›Paper›PMID 42912922›Full record

ArticleJournal of chemical information and modeling2026

GDEE: A Structure-Based Platform for Gene Discovery and Enzyme Engineering.

Caio S Souza, João P G Correia, Isabel Rocha, Diana Lousa, Cláudio M Soares

Abstract read
In one paragraph

Article in Journal of chemical information and modeling, 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

5 authors.

Caio S SouzaInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157Oeiras, Portugal.
João P G CorreiaInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157Oeiras, Portugal.
Isabel RochaInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157Oeiras, Portugal.
Diana LousaInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157Oeiras, Portugal.ORCID 0000-0002-2309-0980
Cláudio M SoaresInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157Oeiras, Portugal.ORCID 0000-0003-1154-556X

Funding

European Commission (Horizon Europe Framework Programme) HORIZON-CL6-2025-01-CIRCBIO-08 ORIGIN - OptFunda??o para a Ci?ncia e a Tecnologia LS4FUTURE Associated Laboratory LA/P/0087/2020 (DOFunda??o para a Ci?ncia e a Tecnologia MOSTMICRO-ITQB R&D Unit UID/04612/2025 (DOI: 10.54Funda??o para a Ci?ncia e a Tecnologia PhD fellowship (2024.01430.BDANA)Horizon 2020 European Commission (EC) H2020-NMBP-BIO-2018 SHIKIFACTORY100 - Modular c
6 · The paper itself

Abstract

Enzymes are extensively utilized for catalyzing the production of value-added compounds in diverse sectors with significant economic impact. However, challenges such as poor protein expression, low catalytic activity, substrate/co-factor limitations, and toxicity of final products limit the efficiency of these biocatalysts. Protein engineering offers a solution by redesigning enzyme catalytic properties to enhance biosynthetic pathways. In this study, we present an automated platform for gene discovery and enzyme engineering, aimed at overcoming these bottlenecks. The GDEE platform finds and optimizes enzymes responsible for rate-limiting steps in biosynthetic pathways, with objectives ranging from improving catalytic efficiency to enabling novel transformations. The platform operates through four key steps: an initial sequence step that either sources natural enzyme sequences or generates mutant variants, followed by an atomistic protein structure prediction step, a docking step, and a binding energy evaluator, obtaining a set of variant enzyme sequences that are prioritized for experimental validation. Additionally, machine learning-based re-scoring of binding poses to improve binding affinities significantly enhances the accuracy of predicting the effect of mutations on binding, highlighting its potential in metabolic engineering applications.

Indexed as

EnzymesProtein EngineeringMachine LearningMutationProtein ConformationEnzymes

Identifiers

PMID42912922
PMCPMC13663853

What OpenQuestion holds

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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.