Seleninate in place of phosphate: irreversible inhibition of protein tyrosine phosphatases.
A homotyrosine based seleninic acid irreversibly inhibits protein tyrosine phosphatases by forming a covalent selenosulfide linkage with the active site cysteine sulfhydryl specifically. The details of the event are revealed by model synthetic studies and by kinetic, mass spectrometric, and crystallographic characterization.
Abdo
Mohannad
M
Department of Chemistry and Chemical Biology, Rutgers The State University of New Jersey, Piscataway, New Jersey 08854, USA.
Liu
Sijiu
S
Zhou
Bo
B
Walls
Chad D
CD
Wu
Li
L
Knapp
Spencer
S
Zhang
Zhong-Yin
ZY
D020240:Apraxia, Ideomotor; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D015394:Molecular Structure; D010710:Phosphates / Q000737:chemistry*; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D018036:Selenium Compounds / Q000737:chemistry* / Q000494:pharmacology*
D010710:Phosphates; D018036:Selenium Compounds; D017027:Protein Tyrosine Phosphatases