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Enzymes and Enzyme Inhibitors in Drug Research
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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
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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 8.3 2011 16.9 Days CHF 2700 Submit
Chemistry
chemistry 		2.1 2.5 2019 19.1 Days CHF 1800 Submit
International Journal of Molecular Sciences
ijms 		5.6 7.8 2000 16.3 Days CHF 2900 Submit
Molecules
molecules 		4.6 6.7 1996 14.6 Days CHF 2700 Submit
Pharmaceuticals
pharmaceuticals 		4.6 4.7 2004 14.6 Days CHF 2900 Submit

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Published Papers (1 paper)

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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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