Literature DB >> 24652175

Biochemical characterization of the bifunctional enzyme dihydrofolate reductase-thymidylate synthase from Leishmania (Viannia) and its evaluation as a drug target.

Edison Osorio1, Carolina Aguilera2, Nelson Naranjo3, Marcel Marín3, Carlos Muskus3.   

Abstract

INTRODUCTION: Dihydrofolate reductase (DHFR) has been used successfully as a drug target in the area of anti-bacterial, anti-cancer and anti-malarial therapy. Although this bifunctional enzyme is also a potential drug target for treatment of leishmaniasis, there have been no reports on its efficacy against Leishmania (Viannia) species.
MATERIALS AND METHODS: The gene encoding the bifunctional DHFR and thymidylate synthase (TS) of Le. (V.) braziliensis was isolated and expressed in E. coli. The enzyme was purified and characterized. The inhibitory effects of antifolates and four aporphine alkaloids on its activity were evaluated.
RESULTS: The full-length gene consists of a 1560-bp open reading frame encoding a 58 kDa translated peptide containing DHFR and TS domains linked together in a single polypeptide chain. The recombinant DHFR-TS enzyme revealed Km and Vmax values of 55.35 ± 4.02 µ M (mean ± SE) and 0.02 ± 5.34 x 10 -4 µ M/min respectively for dihydrofolic acid (H₂F). The Le. braziliensis rDHFR-TS have Ki values for antimicrobial antifolates in the µM range. Methotrexate (MTX) was a more-potent inhibitor of enzymatic activity (Ki = 22.0 µM) than trimethoprim (Ki = 33 µM) and pyrimethamine (Ki = 68 µM). These Ki values are significantly lower than those obtained for the aporphine alkaloids.
CONCLUSION: The results of the study show the inhibitory effect of antifolate drugs on enzymatic activity, indicating that Le. braziliensis rDHFR-TS could be a model to studying antifolate compounds as potential antiprotozoal drugs.

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Year:  2013        PMID: 24652175     DOI: 10.7705/biomedica.v33i3.1434

Source DB:  PubMed          Journal:  Biomedica        ISSN: 0120-4157            Impact factor:   0.935


  4 in total

Review 1.  Dihydrofolate reductase, thymidylate synthase, and serine hydroxy methyltransferase: successful targets against some infectious diseases.

Authors:  Hina Shamshad; Rowaida Bakri; Agha Zeeshan Mirza
Journal:  Mol Biol Rep       Date:  2022-03-07       Impact factor: 2.742

2.  Dual and selective inhibitors of pteridine reductase 1 (PTR1) and dihydrofolate reductase-thymidylate synthase (DHFR-TS) from Leishmania chagasi.

Authors:  Bárbara Velame Ferreira Teixeira; André Lacerda Braga Teles; Suellen Gonçalves da Silva; Camila Carane Bitencourt Brito; Humberto Fonseca de Freitas; Acássia Benjamim Leal Pires; Thamires Quadros Froes; Marcelo Santos Castilho
Journal:  J Enzyme Inhib Med Chem       Date:  2019-12       Impact factor: 5.051

3.  Antileishmanial activity of a series of N²,N⁴-disubstituted quinazoline-2,4-diamines.

Authors:  Kurt S Van Horn; Xiaohua Zhu; Trupti Pandharkar; Sihyung Yang; Brian Vesely; Manu Vanaerschot; Jean-Claude Dujardin; Suman Rijal; Dennis E Kyle; Michael Zhuo Wang; Karl A Werbovetz; Roman Manetsch
Journal:  J Med Chem       Date:  2014-06-17       Impact factor: 7.446

4.  Computational Drug Repositioning for Chagas Disease Using Protein-Ligand Interaction Profiling.

Authors:  Alfredo Juárez-Saldivar; Michael Schroeder; Sebastian Salentin; V Joachim Haupt; Emma Saavedra; Citlali Vázquez; Francisco Reyes-Espinosa; Verónica Herrera-Mayorga; Juan Carlos Villalobos-Rocha; Carlos A García-Pérez; Nuria E Campillo; Gildardo Rivera
Journal:  Int J Mol Sci       Date:  2020-06-16       Impact factor: 5.923

  4 in total

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