Complete replacement set of amino acids at the C-terminus of thymidylate synthase: quantitative structure-activity relationship of mutants of an enzyme
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00141a011
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1. Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis;Nature Chemical Biology;2014-08-17
2. The Role of Protein Dynamics in Thymidylate Synthase Catalysis: Variants of Conserved 2‘-Deoxyuridine 5‘-Monophosphate (dUMP)-Binding Tyr-261,;Biochemistry;2006-05-23
3. Function and Evolution of Plasmid-Borne Genes for Pyrimidine Biosynthesis in Borrelia spp;Journal of Bacteriology;2006-02
4. Crystal structures of thymidylate synthase mutant R166Q: Structural basis for the nearly complete loss of catalytic activity;Journal of Biochemical and Molecular Toxicology;2006
5. The structural roles of conserved Pro196, Pro197 and His199 in the mechanism of thymidylate synthase;Protein Engineering Design and Selection;2003-08-01
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