ArticlePloS one2015
Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Predicting the prognosis of hepatocellular carcinoma based on genes related to polyamine metabolism.PeerJ · 2025Article
- Aldo-keto reductase (AKR) superfamily website and database: An update.Chemico-biological interactions · 2024Article
- Cancer to Cataracts: The Mechanistic Impact of Aldo-Keto Reductases in Chronic Diseases.The Yale journal of biology and medicine · 2024Review
- The pan-cancer landscape of aldo-keto reductase1B10 reveals that its expression is diminished in gastric cancer.Frontiers in immunology · 2024Article
- AKR1B10 and digestive tumors development: a review.Frontiers in immunology · 2024Review
- Aldo-keto reductases: Role in cancer development and theranostics.Oncology research · 2024Review
- Investigating the prognostic value of mTORC1 signaling in bladder cancer via bioinformatics evaluation.Scientific reports · 2023Article
- Perspective on the Structural Basis for Human Aldo-Keto Reductase 1B10 Inhibition.Metabolites · 2021Review
- The Role of AKR1B10 in Physiology and Pathophysiology.Metabolites · 2021Review
- Cancer stem cell transcriptome landscape reveals biomarkers driving breast carcinoma heterogeneity.Breast cancer research and treatment · 2021Article
- Systematically characterize the substance basis of Jinzhen oral liquid and their pharmacological mechanism using UPLC-Q-TOF/MS combined with network pharmacology analysis.Journal of food and drug analysis · 2019Article
- AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders.Molecular and cellular endocrinology · 2019Review
- Aldo-Keto Reductase Family 1 Member B10 Inhibitors: Potential Drugs for Cancer Treatment.Recent patents on anti-cancer drug discovery · 2016Review
- Aldo-Keto Reductases 1B in Adrenal Cortex Physiology.Frontiers in endocrinology · 2016Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human aldo-keto reductase 1B15 (AKR1B15) is a newly discovered enzyme which shares 92% amino acid sequence identity with AKR1B10. While AKR1B10 is a well characterized enzyme with high retinaldehyde reductase activity, involved in the development of several cancer types, the enzymatic activity and physiological role of AKR1B15 are still poorly known. Here, the purified recombinant enzyme has been subjected to substrate specificity characterization, kinetic analysis and inhibitor screening, combined with structural modeling. AKR1B15 is active towards a variety of carbonyl substrates, including retinoids, with lower kcat and Km values than AKR1B10. In contrast to AKR1B10, which strongly prefers all-trans-retinaldehyde, AKR1B15 exhibits superior catalytic efficiency with 9-cis-retinaldehyde, the best substrate found for this enzyme. With ketone and dicarbonyl substrates, AKR1B15 also shows higher catalytic activity than AKR1B10. Several typical AKR inhibitors do not significantly affect AKR1B15 activity. Amino acid substitutions clustered in loops A and C result in a smaller, more hydrophobic and more rigid active site in AKR1B15 compared with the AKR1B10 pocket, consistent with distinct substrate specificity and narrower inhibitor selectivity for AKR1B15.
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