Global Kinetic Mechanism of Microsomal Glutathione Transferase 1 and Insights into Dynamic Enzyme Activation.

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Spahiu L, Ålander J, Ottosson-Wadlund A, Svensson R, Lehmer C, Armstrong RN, Morgenstern R

Biochemistry 56 (24) 3089-3098 [2017-06-20; online 2017-06-09]

Microsomal glutathione transferase 1 (MGST1) has a unique ability to be activated, ≤30-fold, by modification with sulfhydryl reagents. MGST1 exhibits one-third-of-the-sites reactivity toward glutathione and hence heterogeneous binding to different active sites in the homotrimer. Limited turnover stopped-flow kinetic measurements of the activated enzyme allowed us to more accurately determine the K

Affiliated researcher

PubMed 28558199

DOI 10.1021/acs.biochem.7b00285

Crossref 10.1021/acs.biochem.7b00285

pmc: PMC5954419
mid: NIHMS964830