Cited by 171Redox biology and oxidative stressNitric Oxide and Endothelin EffectsAmino Acid Enzymes and Metabolism

Peroxynitrite-mediated nitration of tyrosine residues in Escherichia coli glutamine synthetase mimics adenylylation: Relevance to signal transduction

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Berlett, B S, Friguet, B, Yim, M B, Chock, P B, Stadtman, E R·1996·Proceedings of the National Academy of Sciences

Abstract

Treatment of Escherichia coli glutamine synthetase (GS) with peroxynitrite leads to nitration of some tyrosine residues and conversion of some methionine residues to methionine sulfoxide (MSOX) residues. Nitration, but not MSOX formation, is stimulated by Fe-EDTA. In the absence of Fe-EDTA, nitration of only one tyrosine residue per subunit of unadenylylated GS leads to changes in divalent cation requirement, pH-activity profile, affinity for ADP, and susceptibility to feedback inhibition by end products (tryptophan, AMP, CTP), whereas nitration of one tyrosine residue per subunit in the adenylylated GS leads to complete loss of catalytic activity. In the presence of Fe-EDTA, nitration is a more random process: nitration of five to six tyrosine residues per subunit is needed to convert unadenylylated GS to the adenylylated configuration. These results and the fact that nitration of tyrosine residues is an irreversible process serve notice that the regulatory function of proteins that undergo phosphorylation or adenylylation in signal transduction cascades might be seriously compromised by peroxynitrite-promoted nitration.

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Crossref · 10.1073/pnas.93.5.1776

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Authors
Berlett, B. S., Friguet, B., Yim, M. B., Chock, P. B., & Stadtman, E. R.
Affiliations
National Institutes of Health (US)
Venue
Proceedings of the National Academy of Sciences
Published
1996-03-05
Volume
93
Issue
5
Pages
1776-1780
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1970184469
Cited by
171
References
14
Citations by year
2024: 2 · 2023: 4 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 3 · 2017: 1 · 2016: 2 · 2015: 1 · 2014: 8 · 2013: 6 · 2012: 3
FWCI
6.94
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords
peroxynitrite, tyrosine nitration, glutamine synthetase, adenylylation, methionine sulfoxide, Fe-EDTA, protein regulation, signal transduction, enzyme activity, product inhibition, ADP binding, Escherichia coli
MeSH terms
Cations, Divalent, Escherichia coli, Glutamate-Ammonia Ligase, Manganese, Methionine, Nitrates, Structure-Activity Relationship, Tyrosine, Signal Transduction

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