Evidence map›Paper›PMID 41940686›Full record

ArticleProtein science : a publication of the Protein Society2026

Hydrophobic interactions of a substrate with L193 on the flexible substrate-binding loop contribute to 3α-hydroxysteroid dehydrogenase/carbonyl reductase catalytic efficiency.

Yan-Liang Chen, Yun-Hao Chou, Hwei-Jen Lee, Tzu-Pin Wang, Chi-Ching Hwang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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.

Yan-Liang ChenDepartment of Biochemistry, Faculty of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
Yun-Hao ChouGraduate Institute of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
Hwei-Jen LeeGraduate Institute of Biochemistry, College of Biomedical Science, National Defense Medical University, Taipei, Taiwan.
Tzu-Pin WangDepartment of Medicinal and Applied Chemistry, Kaohsiung Medical University, Kaohsiung, Taiwan.
Chi-Ching HwangDepartment of Biochemistry, Faculty of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.

Funding

Kaohsiung Medical University KMU-M113002Kaohsiung Medical University KMU-M114001
6 · The paper itself

Abstract

Flexible loops within enzyme active sites are central to substrate binding, transition-state stabilization, and catalytic turnover. Hydrophobic interactions modulate ligand recognition and influence protein function. Here, we interrogated loop-mediated hydrophobic contributions to catalysis in 3α-hydroxysteroid dehydrogenase/carbonyl reductase (3α-HSD/CR) from Comamonas testosteroni. Residue L193 on the flexible substrate-binding loop was substituted with amino acids spanning a hydrophobicity gradient (W, I, F, M, V, P, A, T, G). Differential scanning fluorimetry showed comparable melting temperatures among variants, indicating minimal effects on global thermal stability. Steady-state kinetics revealed decreased catalytic efficiency with reduced side-chain hydrophobicity and corresponding increases in activation free energy (ΔG

Indexed as

Alcohol OxidoreductasesBacterial ProteinsComamonas testosteroniCatalytic DomainHydrophobic and Hydrophilic InteractionsHydroxysteroid DehydrogenasesKineticsSubstrate Specificity3alpha-hydroxysteroid dehydrogenase-carbonyl reductaseAlcohol OxidoreductasesBacterial ProteinsHydroxysteroid Dehydrogenasesenzyme catalysisGibbs free energy changehydrophobic interactionremote binding interactionsteady‐state kineticssubstrate‐binding loopthermal stability

Identifiers

PMID41940686
PMCPMC13051958

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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.