Inhibition of the lymphoid tyrosine phosphatase: The effect of zinc(II) ions and chelating ligand fragments on enzymatic activity

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Author list: Thorson MK, Puerta DT, Cohen SM, Barrios AM
Publisher: Elsevier
Publication year: 2014
Volume number: 24
Issue number: 16
Start page: 4019
End page: 4022
Number of pages: 4
ISSN: 0960-894X
Languages: English-Great Britain (EN-GB)


A 96-member chelator fragment library (CFL-1.1) was screened to identify inhibitors of the lymphoid tyrosine phosphatase in the absence and presence of zinc acetate. Fragments that inhibit LYP activity more potently in the presence of zinc, fragments that rescue LYP activity in the presence of inhibitory concentrations of zinc, and fragments that inhibit LYP activity independent of zinc concentration were identified. Of these, 1,2-dihydroxynaphthalene was the most potent inhibitor with an IC50 value of 2.52 +/- 0.06 mu M after 2 h of incubation. LYP inhibition by 1,2-dihydroxynaphthalene was very similar to inhibition by 1,2-naphthoquinone (IC50 = 1.10 +/- 0.03 mu M), indicating that the oxidized quinone species is likely the active inhibitor. The inhibition was time-dependent, consistent with covalent modification of the enzyme. (C) 2014 Elsevier Ltd. All rights reserved.


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Last updated on 2019-23-08 at 11:15