Single Residue on the WPD-Loop Affects the pH Dependency of Catalysis in Protein Tyrosine Phosphatases
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322-0300, United States
2. Science for Life Laboratory, Department of Chemistry − BMC, Uppsala University, Box 576, S-751 23 Uppsala, Sweden
Funder
Human Frontier Science Program
Carl Tryggers Foundation for Scientific Research
Knut and Alice Wallenberg Foundation
Swedish Research Council
Publisher
American Chemical Society (ACS)
Subject
General Medicine
Link
https://pubs.acs.org/doi/pdf/10.1021/jacsau.1c00054
Reference57 articles.
1. Structural study reveals the temperature-dependent conformational flexibility of Tk-PTP, a protein tyrosine phosphatase from Thermococcus kodakaraensis KOD1
2. Receptor protein-tyrosine phosphatase gamma is a candidate tumor suppressor gene at human chromosome region 3p21.
3. Protein tyrosine phosphatases: mechanisms of catalysis and regulation
4. Molecular Reactions of Protein PhosphatasesInsights from Structure and Chemistry
5. Protein Tyrosine Phosphatases: Structure and Function, Substrate Specificity, and Inhibitor Development
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