ijms-logo

Journal Browser

Journal Browser

Research of Aldo-Keto Reductases in Human Disease

A Special Issue of International Journal of Molecular Sciences (ISSN 1422-0067) belonging to the section "Biochemistry".

Deadline for manuscript submissions: 30 November 2026 | Viewed by 582

Editors

College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
Interests: enzyme antioxidants

E-Mail Website
Guest Editor Assistant
College of Life Science, Northeast Forestry University, Harbin 150040, China
Interests: enzyme engineering

Special Issue Information

Dear Colleagues,

The aldo-keto reductase (AKR) superfamily comprises NAD(P)H-dependent oxidoreductases that catalyze the reduction of a broad spectrum of carbonyl substrates, including aldehydes, ketones, quinones, and steroids. Members of this superfamily—particularly AKR1B1 (aldose reductase), AKR1B10, and the AKR1C subfamily—play pivotal roles in numerous pathophysiological processes, such as diabetic complications, tumorigenesis and cancer progression, chemoresistance, steroid hormone metabolism, lipid peroxidation, oxidative stress, and inflammatory responses. Recent advances in structural biology, protein engineering, molecular pharmacology, and translational medicine have substantially deepened our understanding of AKR biology and revealed new opportunities for therapeutic intervention and biocatalytic application. This Special Issue aims to cover state-of-the-art research on the basic, applied, and clinical aspects of AKRs in human disease. We invite authors to submit original articles and review articles addressing recent findings on AKR enzymology, regulation, engineering, and disease relevance. Potential topics include, but are not limited to: Structural and functional characterization of AKR enzymes Protein engineering and directed evolution of AKRs for enhanced activity, stereoselectivity, or substrate specificity Rational design and semi-rational engineering of AKR active sites for biomedical and biocatalytic applications AKRs as diagnostic, prognostic, or therapeutic biomarkers in human cancers Roles of AKRs in chemoresistance and xenobiotic metabolism Design and evaluation of AKR inhibitors for clinical application AKRs in diabetic complications and metabolic disorders AKRs in steroid hormone metabolism and hormone-dependent diseases AKRs in oxidative stress, lipid peroxidation, and inflammation Genetic polymorphisms of AKRs and their clinical significance.

Dr. Ping Zhu
Guest Editor

Dr. Hao Luo
Guest Editor Assistant

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-anonymized peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • aldo-keto reductase (AKR)
  • protein engineering
  • AKR1B10
  • cancer biomarker
  • chemoresistance

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

15 pages, 1476 KB  
Article
Rational Engineering of AKR13B3 from Devosia A6-243 for Enhanced Aflatoxin B1 Degradation: A Dual Mechanism of Substrate Polarization and Tunnel Remodeling
by Qingwei Jiang, Juan Shen, Zhanghu Chen, Xiaoqing Zhu, Caiyi Chen, Hao Zhu, Huibing Chi, Fengxia Lu and Ping Zhu
Int. J. Mol. Sci. 2026, 27(16), 7380; https://doi.org/10.3390/ijms27167380 - 18 Aug 2026
Viewed by 344
Abstract
Aflatoxin B1 (AFB1) is one of the most toxic mycotoxins, widely contaminating agricultural products and posing a serious threat to food safety and human health. Enzymatic degradation is considered a promising detoxification strategy due to its high efficiency, strong specificity, and lack of [...] Read more.
Aflatoxin B1 (AFB1) is one of the most toxic mycotoxins, widely contaminating agricultural products and posing a serious threat to food safety and human health. Enzymatic degradation is considered a promising detoxification strategy due to its high efficiency, strong specificity, and lack of secondary pollution. AKR13B3, a member of the aldo-keto reductase family, possesses intrinsic catalytic activity for AFB1 degradation; however, its low natural activity severely limits practical application. In this study, the binding mode of the AKR13B3-NADPH complex with AFB1 was first determined using AlphaFold 3.0 and AutoDock Vina. Through interaction analysis, Trp102 and Asp41 were identified as key targets for enhancing catalytic activity. Following site-directed mutagenesis screening, two mutants, D41H and D41T, with significantly improved catalytic activity were obtained, exhibiting 52.32% and 46.44% higher activity than the wild-type enzyme, respectively. Three-dimensional structural simulation revealed that D41H and D41T form stable interactions with the carbonyl group on the lactone ring of AFB1, thereby polarizing the carbonyl group and reducing the activation energy of the reaction, ultimately enhancing catalytic activity. Substrate channel analysis demonstrated that, compared with the wild-type, the D41H and D41T mutants significantly increased the bottleneck radius of the substrate channel (by 25% and 22%, respectively) and shortened the channel length (by 23% and 33%, respectively), thereby partially relieving steric hindrance and diffusion limitations and improving catalytic efficiency. In summary, this study elucidates the molecular basis by which D41H and D41T enhance the catalytic activity of AKR13B3 toward AFB1 through the dual mechanisms of external/hydrogen bond catalysis and channel remodeling, providing an important theoretical foundation for the rational design and directed engineering of AFB1-degrading enzymes. Full article
(This article belongs to the Special Issue Research of Aldo-Keto Reductases in Human Disease)
Show Figures

Figure 1

Back to TopTop