Evidence map›Paper›PMID 38189538›Full record

ArticleBriefings in bioinformatics2023

DLTKcat: deep learning-based prediction of temperature-dependent enzyme turnover rates.

Sizhe Qiu, Simiao Zhao, Aidong Yang

Abstract read
In one paragraph

Article in Briefings in bioinformatics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Enhancing kCommunications biology · 2026
    Article
  2. Advances in Machine Learning Models for Predicting Enzyme Kinetic Parameters.Journal of chemical information and modeling · 2026
    Review
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  6. Rubisco is slow across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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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

3 authors.

Sizhe QiuDepartment of Engineering Science, University of Oxford, OX1 3PJ, United Kingdom.ORCID 0000-0002-1936-1223
Simiao ZhaoRadcliffe Department of Medicine, University of Oxford, OX3 9DU, United Kingdom.
Aidong YangDepartment of Engineering Science, University of Oxford, OX1 3PJ, United Kingdom.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme turnover rate, ${k}_{cat}$, quantifies enzyme kinetics by indicating the maximum efficiency of enzyme catalysis. Despite its importance, ${k}_{cat}$ values remain scarce in databases for most organisms, primarily because of the cost of experimental measurements. To predict ${k}_{cat}$ and account for its strong temperature dependence, DLTKcat was developed in this study and demonstrated superior performance (log10-scale root mean squared error = 0.88, R-squared = 0.66) than previously published models. Through two case studies, DLTKcat showed its ability to predict the effects of protein sequence mutations and temperature changes on ${k}_{cat}$ values. Although its quantitative accuracy is not high enough yet to model the responses of cellular metabolism to temperature changes, DLTKcat has the potential to eventually become a computational tool to describe the temperature dependence of biological systems.

Indexed as

Deep LearningAmino Acid SequenceCatalysisDatabases, FactualTemperaturecompound–protein interactiondeep learningenzyme turnover rategenome-scale metabolic modelingtemperature dependence

Identifiers

PMID38189538
PMCPMC10772988

What OpenQuestion holds

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LicenceCC BY
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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.