[29] Redox regulation of protein tyrosine phosphatases by hydrogen peroxide: Detecting sulfenic acid intermediates and examining reversible inactivation
JM Denu, KG Tanner - Methods in enzymology, 2002 - Elsevier
Publisher Summary This chapter describes a mechanism of redox reduction for protein
tyrosine phosphatases (PTPs) in which the transient intracellular production of hydrogen
peroxide, as a result of growth factor/mitogen stimulation of cell surface receptors, leads to
the rapid inactivation of PTPs by the modification of their invariant catalytic cysteine thiolate
(R–S) to an inactive sulfenic acid (R–SOH). The chapter describes methods to test if specific
PTPs can be regulated by reversible inactivation with hydrogen peroxide. These techniques …
tyrosine phosphatases (PTPs) in which the transient intracellular production of hydrogen
peroxide, as a result of growth factor/mitogen stimulation of cell surface receptors, leads to
the rapid inactivation of PTPs by the modification of their invariant catalytic cysteine thiolate
(R–S) to an inactive sulfenic acid (R–SOH). The chapter describes methods to test if specific
PTPs can be regulated by reversible inactivation with hydrogen peroxide. These techniques …