Topic Editors

School of Pharmacy, Aristotle University of Thessaloniki, Thessaloniki, Greece
Department of Pharmacy-Pharmaceutical Sciences, University of Bari, Bari, Italy
Department of Pharmacy, Health and Nutritional Sciences, University of Calabria, Arcavacata, Italy

Enzymes and Enzyme Inhibitors in Drug Research

Abstract submission deadline
31 October 2025
Manuscript submission deadline
31 December 2025
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Topic Information

Dear Colleagues,

Enzymes are involved in many pathological conditions, such as inflammation, diabetes, microbial infections, HIV, neoplastic diseases and others. Enzyme inhibition is universally accepted as a strategy to treat the above-mentioned conditions or to reverse the mechanism involved. In the long drug development process, the design of potent enzyme inhibitors is a crucial step. This Topic is dedicated to enzymes and their inhibition in drug design and development; these may include HIV-1 RT, transcriptase, SAR CoV-2, PTP1B, LOX, COX carbonic anhydrase, aldose reductase, and many others.

We welcome relevant original research, reviews, and other articles that cover (but are not limited to) the following subjects:

  • The role of enzymes in many pathological conditions;
  • Strategies for the development of enzyme inhibitors;
  • Targets for the development of new drugs, as well as the role of computational chemistry in drug design.

Prof. Dr. Athina Geronikaki
Prof. Dr. Cosimo D. Altomare
Prof. Dr. Maria Stefania Sinicropi
Topic Editors

Keywords

  • enzymes
  • inhibitors of HIV
  • SARS Cov-2
  • PTP1B
  • SHP2
  • LOX
  • COX
  • CA
  • aldose reductase
  • kinase inhibitors
  • gyrase
  • primase

Participating Journals

Journal Name Impact Factor CiteScore Launched Year First Decision (median) APC
Biomolecules
biomolecules
5.5 9.4 2011 16.9 Days CHF 2700 Submit
Chemistry
chemistry
2.1 3.2 2019 19.1 Days CHF 1800 Submit
International Journal of Molecular Sciences
ijms
5.6 8.1 2000 16.3 Days CHF 2900 Submit
Molecules
molecules
4.6 7.4 1996 14.6 Days CHF 2700 Submit
Pharmaceuticals
pharmaceuticals
4.6 6.1 2004 14.6 Days CHF 2900 Submit

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Published Papers (3 papers)

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31 pages, 3154 KiB  
Review
Exploring Therapeutic Potential of Catalase: Strategies in Disease Prevention and Management
by Shehwaz Anwar, Faris Alrumaihi, Tarique Sarwar, Ali Yousif Babiker, Amjad Ali Khan, Sitrarasu Vijaya Prabhu and Arshad Husain Rahmani
Biomolecules 2024, 14(6), 697; https://doi.org/10.3390/biom14060697 - 14 Jun 2024
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Abstract
The antioxidant defense mechanisms play a critical role in mitigating the deleterious effects of reactive oxygen species (ROS). Catalase stands out as a paramount enzymatic antioxidant. It efficiently catalyzes the decomposition of hydrogen peroxide (H2O2) into water and oxygen, [...] Read more.
The antioxidant defense mechanisms play a critical role in mitigating the deleterious effects of reactive oxygen species (ROS). Catalase stands out as a paramount enzymatic antioxidant. It efficiently catalyzes the decomposition of hydrogen peroxide (H2O2) into water and oxygen, a potentially harmful byproduct of cellular metabolism. This reaction detoxifies H2O2 and prevents oxidative damage. Catalase has been extensively studied as a therapeutic antioxidant. Its applications range from direct supplementation in conditions characterized by oxidative stress to gene therapy approaches to enhance endogenous catalase activity. The enzyme’s stability, bioavailability, and the specificity of its delivery to target tissues are significant hurdles. Furthermore, studies employing conventional catalase formulations often face issues related to enzyme purity, activity, and longevity in the biological milieu. Addressing these challenges necessitates rigorous scientific inquiry and well-designed clinical trials. Such trials must be underpinned by sound experimental designs, incorporating advanced catalase formulations or novel delivery systems that can overcome existing limitations. Enhancing catalase’s stability, specificity, and longevity in vivo could unlock its full therapeutic potential. It is necessary to understand the role of catalase in disease-specific contexts, paving the way for precision antioxidant therapy that could significantly impact the treatment of diseases associated with oxidative stress. Full article
(This article belongs to the Topic Enzymes and Enzyme Inhibitors in Drug Research)
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19 pages, 4015 KiB  
Article
In Vitro and Molecular Docking Evaluation of the Anticholinesterase and Antidiabetic Effects of Compounds from Terminalia macroptera Guill. & Perr. (Combretaceae)
by Romeo Toko Feunaing, Alfred Ngenge Tamfu, Abel Joel Yaya Gbaweng, Selcuk Kucukaydin, Joseph Tchamgoue, Alain Meli Lannang, Bruno Ndjakou Lenta, Simeon Fogue Kouam, Mehmet Emin Duru, El Hassane Anouar, Emmanuel Talla and Rodica Mihaela Dinica
Molecules 2024, 29(11), 2456; https://doi.org/10.3390/molecules29112456 - 23 May 2024
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Abstract
Alzheimer’s disease (AD) and diabetes are non-communicable diseases with global impacts. Inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are suitable therapies for AD, while α-amylase and α-glucosidase inhibitors are employed as antidiabetic agents. Compounds were isolated from the medicinal plant Terminalia macroptera and [...] Read more.
Alzheimer’s disease (AD) and diabetes are non-communicable diseases with global impacts. Inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are suitable therapies for AD, while α-amylase and α-glucosidase inhibitors are employed as antidiabetic agents. Compounds were isolated from the medicinal plant Terminalia macroptera and evaluated for their AChE, BChE, α-amylase, and α-glucosidase inhibitions. From 1H and 13C NMR data, the compounds were identified as 3,3′-di-O-methyl ellagic acid (1), 3,3′,4′-tri-O-methyl ellagic acid-4-O-β-D-xylopyranoside (2), 3,3′,4′-tri-O-methyl ellagic acid-4-O-β-D-glucopyranoside (3), 3,3′-di-O-methyl ellagic acid-4-O-β-D-glucopyranoside (4), myricetin-3-O-rhamnoside (5), shikimic acid (6), arjungenin (7), terminolic acid (8), 24-deoxysericoside (9), arjunglucoside I (10), and chebuloside II (11). The derivatives of ellagic acid (14) showed moderate to good inhibition of cholinesterases, with the most potent being 3,3′-di-O-methyl ellagic acid, with IC50 values of 46.77 ± 0.90 µg/mL and 50.48 ± 1.10 µg/mL against AChE and BChE, respectively. The compounds exhibited potential inhibition of α-amylase and α-glucosidase, especially the phenolic compounds (15). Myricetin-3-O-rhamnoside had the highest α-amylase inhibition with an IC50 value of 65.17 ± 0.43 µg/mL compared to acarbose with an IC50 value of 32.25 ± 0.36 µg/mL. Two compounds, 3,3′-di-O-methyl ellagic acid (IC50 = 74.18 ± 0.29 µg/mL) and myricetin-3-O-rhamnoside (IC50 = 69.02 ± 0.65 µg/mL), were more active than the standard acarbose (IC50 = 87.70 ± 0.68 µg/mL) in the α-glucosidase assay. For α-glucosidase and α-amylase, the molecular docking results for 1–11 reveal that these compounds may fit well into the binding sites of the target enzymes, establishing stable complexes with negative binding energies in the range of −4.03 to −10.20 kcalmol−1. Though not all the compounds showed binding affinities with cholinesterases, some had negative binding energies, indicating that the inhibition was thermodynamically favorable. Full article
(This article belongs to the Topic Enzymes and Enzyme Inhibitors in Drug Research)
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9 pages, 1517 KiB  
Article
Pre-Steady-State and Steady-State Kinetic Analysis of Butyrylcholinesterase-Catalyzed Hydrolysis of Mirabegron, an Arylacylamide Drug
by Zukhra Shaihutdinova and Patrick Masson
Molecules 2024, 29(10), 2356; https://doi.org/10.3390/molecules29102356 - 16 May 2024
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Abstract
The β-adrenergic drug Mirabegron, a drug initially used for the treatment of an overactive bladder, has new potential indications and is hydrolyzed by butyrylcholinesterase (BChE). This compound is one of the only arylacylamide substrates to be catabolized by BChE. A steady-state kinetic analysis [...] Read more.
The β-adrenergic drug Mirabegron, a drug initially used for the treatment of an overactive bladder, has new potential indications and is hydrolyzed by butyrylcholinesterase (BChE). This compound is one of the only arylacylamide substrates to be catabolized by BChE. A steady-state kinetic analysis at 25 °C and pH 7.0 showed that the enzyme behavior is Michaelian with this substrate and displays a long pre-steady-state phase characterized by a burst. The induction time, τ, increased with substrate concentration (τ ≈ 18 min at maximum velocity). The kinetic behavior was interpreted in terms of hysteretic behavior, resulting from a slow equilibrium between two enzyme active forms, E and E′. The pre-steady-state phase with the highest activity corresponds to action of the E form, and the steady state corresponds to action of the E′ form. The catalytic parameters were determined as kcat = 7.3 min−1 and Km = 23.5 μM for the initial (burst) form E, and kcat = 1.6 min−1 and Km = 3.9 μM for the final form E′. Thus, the higher affinity of E′ for Mirabegron triggers the slow enzyme state equilibrium toward a slow steady state. Despite the complexity of the reaction mechanism of Mirabegron with BChE, slow BChE-catalyzed degradation of Mirabegron in blood should have no impact on the pharmacological activities of this drug. Full article
(This article belongs to the Topic Enzymes and Enzyme Inhibitors in Drug Research)
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