Inactivation of protein tyrosine phosphatases by dietary isothiocyanates
Sarah M Lewis1, Ya Li2, Michael J Catalano1
1University of Missouri, Department of Chemistry, 125 Chemistry Building, Columbia, MO 65211, United States.
Abstract:
Isothiocyanates are bioactive dietary phytochemicals that react readily with protein thiol groups. We find that isothiocyanates are time-dependent inactivators of cysteine-dependent protein tyrosine phosphatases (PTPs). Rate constants for the inactivation of PTP1B and SHP-2 by allyl isothiocyanate and sulforaphane range from 2 to 16 M(-1)s(-1). Results in the context of PTP1B are consistent with a mechanism involving covalent, yet reversible, modification of the enzyme's active site cysteine residue.
Related Concept Videos
The JAK-STAT Signaling Pathway
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Cancer Prevention
Some...
mTOR Signaling and Cancer Progression
The mTOR pathway or the...
Bioactivation and Tissue Toxicity
Amplifying Signals via Enzymatic Cascade


