title: Phosphorylation of tyrosine prevents dityrosine formation in vitro.
abstract: Treatment of L-tyrosine in a peroxidase/H2O2 system results in the formation of dityrosine. However, the phosphoester derivative of tyrosine, O-phospho-L-tyrosine, was unable to form dityrosine even in mixtures with free L-tyrosine. Dephosphorylation of O-phospho-L-tyrosine by alkaline phosphatase followed by horseradish peroxidase/H2O2 treatment resulted in the formation of dityrosine. Our in vitro results indicate that phosphorylation/dephosphorylation of L-tyrosine may regulate dityrosine formation, and is supposed to play an important role in protein-protein interactions, i.e. cross-linking.
authors: Department of Medical Chemistry, University of Vienna, Austria.
authors: B
authors: B
authors: Gmeiner
authors: C
authors: C
authors: Seelos
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D006735:Horseradish Peroxidase / Q000378:metabolism; D007700:Kinetics; D010766:Phosphorylation; D019000:Phosphotyrosine; D014443:Tyrosine / Q000031:analogs & derivatives
chemical_list: D019000:Phosphotyrosine; D014443:Tyrosine; C007543:dityrosine; D006735:Horseradish Peroxidase; D000469:Alkaline Phosphatase