Explaining an Unusually Fast Parasitic Enzyme: Folate Tail-Binding Residues Dictate Substrate Positioning and Catalysis in Cryptosporidium hominis Thymidylate Synthase
Author:
Affiliation:
1. Department of Molecular Biophysics and Biochemistry and Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06520
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi800466z
Reference37 articles.
1. THE CATALYTIC MECHANISM AND STRUCTURE OF THYMIDYLATE SYNTHASE
2. A Perspective on Enzyme Catalysis
3. Mechanism of interaction of thymidylate synthetase with 5-fluorodeoxyuridylate
4. Kinetic Characterization of Bifunctional Thymidylate Synthase-Dihydrofolate Reductase (TS-DHFR) from Cryptosporidium hominis
5. Potential antifolate resistance determinants and genotypic variation in the bifunctional dihydrofolate reductase-thymidylate synthase gene from human and bovine isolates of Cryptosporidium parvum
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1. Bioinformatics Applications on Cryptosporidium Research: A Review;Bangladesh Journal of Medical Science;2022-01-01
2. Structure activity relationship towards design of cryptosporidium specific thymidylate synthase inhibitors;European Journal of Medicinal Chemistry;2019-12
3. Understanding the structural basis of species selective, stereospecific inhibition for Cryptosporidium and human thymidylate synthase;FEBS Letters;2019-06-18
4. Structural studies provide clues for analog design of specific inhibitors of Cryptosporidium hominis thymidylate synthase–dihydrofolate reductase;Bioorganic & Medicinal Chemistry Letters;2014-09
5. Cryptosporidium Species;Genomes of Foodborne and Waterborne Pathogens;2014-04-09
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