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Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site.

Abstract：

: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+ protect against inactivation and modification, in agreement with the study on E. coli dUTPase (Vertessy et al. (1994) Biochim. Biophys. Acta 1205, 146-150). Amino acid analyses of nitrated dUTPases confirmed Tyr-selectivity of modification. The nitrated residue in E. coli dUTPase was identified as the evolutionary highly conserved Tyr-93. The modifiable residue is shown to be the only Tyr exposed in both E. coli and EIAV dUTPases. As a consequence of Tyr-93 derivatization, the Mg2+-dependent interaction between the substrate-analogue dUDP and E. coli dUTPase becomes impaired as shown by circular dichroism spectroscopy, here presented as a tool for monitoring ligand binding to the active site.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Vertessy BG,Persson R,Rosengren AM,Zeppezauer M,Nyman PO

doi

10.1006/bbrc.1996.0226

subject

Has Abstract

pub_date

1996-02-15 00:00:00

pages

294-300

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)90226-0

journal_volume

219

pub_type

杂志文章

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