Specific Derivatization of the Active Site Tyrosine in dUTPase Perturbs Ligand Binding to the Active Site
Selective modification of one (of three) tyrosine residue per enzyme monomer leads to inactivation of dUTPase of the retrovirus equine infectious anemia virus (EIAV). The substrate dUMP and the cofactor Mg2+protects against inactivation and modification, in agreement with the study onE. colidUTPase (Vertessyet al.(1994)Biochim. Biophys. Acta1205, 146-150). Amino acid analyses of nitrated dUTPases