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Specific Derivatization of the Active Site Tyrosine in dUTPase Perturbs Ligand Binding to the Active Site

Vertessy, Beata G; Persson, Rebecca; Rosengren, Anna-Maria; Zeppezauer, Michael and Nyman, Per-Olof LU (1996) In Biochemical and Biophysical Research Communications 219(2). p.294-300
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+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 confirmed Tyr-selectivity of modification. The nitrated residue inE. colidUTPase was identified as the evolutionary highly conserved Tyr-93. The modifiable residue is shown to be the only Tyr exposed in bothE. coliand EIAV dUTPases. As a consequence of Tyr-93 derivatization, the Mg2+-dependent interaction between the substrate-analogue dUDP andE.... (More)
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 confirmed Tyr-selectivity of modification. The nitrated residue inE. colidUTPase was identified as the evolutionary highly conserved Tyr-93. The modifiable residue is shown to be the only Tyr exposed in bothE. coliand EIAV dUTPases. As a consequence of Tyr-93 derivatization, the Mg2+-dependent interaction between the substrate-analogue dUDP andE. colidUTPase becomes impaired as shown by circular dichroism spectroscopy, here presented as a tool for monitoring ligand binding to the active site. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
219
issue
2
pages
294 - 300
publisher
Elsevier
external identifiers
  • scopus:0029874744
ISSN
1090-2104
DOI
10.1006/bbrc.1996.0226
language
English
LU publication?
yes
id
1a8992c8-aabf-4286-8b05-a88eebcae162 (old id 126369)
date added to LUP
2007-07-09 10:43:12
date last changed
2017-01-01 06:52:16
@article{1a8992c8-aabf-4286-8b05-a88eebcae162,
  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+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 confirmed Tyr-selectivity of modification. The nitrated residue inE. colidUTPase was identified as the evolutionary highly conserved Tyr-93. The modifiable residue is shown to be the only Tyr exposed in bothE. coliand EIAV dUTPases. As a consequence of Tyr-93 derivatization, the Mg2+-dependent interaction between the substrate-analogue dUDP andE. colidUTPase becomes impaired as shown by circular dichroism spectroscopy, here presented as a tool for monitoring ligand binding to the active site.},
  author       = {Vertessy, Beata G and Persson, Rebecca and Rosengren, Anna-Maria and Zeppezauer, Michael and Nyman, Per-Olof},
  issn         = {1090-2104},
  language     = {eng},
  number       = {2},
  pages        = {294--300},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Specific Derivatization of the Active Site Tyrosine in dUTPase Perturbs Ligand Binding to the Active Site},
  url          = {http://dx.doi.org/10.1006/bbrc.1996.0226},
  volume       = {219},
  year         = {1996},
}