Kinetics and mechanisms associated with redox regulation of protein tyrosine phosphatase 1B (PTP1B)
No Thumbnail Available
Authors
Meeting name
Sponsors
Date
Journal Title
Format
Thesis
Subject
Abstract
Here, we report on the kinetics and mechanisms associated with redox regulation of the protein tyrosine phosphatase PTP1B. We determined rates of thiol- and phosphinemediated recovery of catalytic activity from the oxidatively-inactivated enzyme, and shed light on the chemical mechanisms involved in these processes and in the regulation of PTP family member SHP2. Additionally, we describe reactions that oxidatively-inactivated PTP1B undergo with structurally-diverse carbon acids, using both a small chemical model dipeptide of oxidatively-inactivated PTP1B, and the oxidized enzyme itself. Finally, we report a novel method by which to predict Hammett substituent constants via electronic structure calculations.
Table of Contents
DOI
PubMed ID
Degree
Ph. D.
Thesis Department
Rights
OpenAccess.
License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License.