Cited by 43Redox biology and oxidative stressSulfur Compounds in BiologySelenium in Biological Systems

Recharging oxidative protein repair: Catalysis by methionine sulfoxide reductases towards their amino acid, protein, and model substrates

Tarrago, L., Gladyshev, V. N.·2012·Biochemistry (Moscow)

Abstract

The sulfur-containing amino acid methionine (Met) in its free and amino acid residue forms can be readily oxidized to the R and S diastereomers of methionine sulfoxide (MetO). Methionine sulfoxide reductases A (MSRA) and B (MSRB) reduce MetO back to Met in a stereospecific manner, acting on the S and R forms, respectively. A third MSR type, fRMSR, reduces the R form of free MetO. MSRA and MSRB are spread across the three domains of life, whereas fRMSR is restricted to bacteria and unicellular eukaryotes. These enzymes protect against abiotic and biotic stresses and regulate lifespan. MSRs are thiol oxidoreductases containing catalytic redox-active cysteine or selenocysteine residues, which become oxidized by the substrate, requiring regeneration for the next catalytic cycle. These enzymes can be classified according to the number of redox-active cysteines (selenocysteines) and the strategies to regenerate their active forms by thioredoxin and glutaredoxin systems. For each MSR type, we review catalytic parameters for the reduction of free MetO, low molecular weight MetO-containing compounds, and oxidized proteins. Analysis of these data reinforces the concept that MSRAs reduce various types of MetO-containing substrates with similar efficiency, whereas MSRBs are specialized for the reduction of MetO in proteins.

Integrity signals

Registry

Crossref · 10.1134/s0006297912100021

Cites

97 of 97 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Cites

Flagged first, then by citations

Research works printed but not linked: 1

  1. Lowther, W. T., Weissbach, H., Etienne, F., Brot, N., and Matthews, B. W. (2002) Nat. Struct. Biol., 9, 348–352.

Cited by

Sorted by citations

Authors
Tarrago, L., & Gladyshev, V. N.
Affiliations
Brigham and Women's Hospital (US)
Corresponding author
Gladyshev, V. N.
Venue
Biochemistry (Moscow)
Published
2012-10
Volume
77
Issue
10
Pages
1097-1107
ISSN
  • 0006-2979 (ISSN-L)
  • 1608-3040
OpenAlex
W2148497496
Cited by
43
References
97
Citations by year
2026: 1 · 2025: 1 · 2023: 2 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 5 · 2017: 3 · 2016: 4 · 2015: 2 · 2014: 3 · 2013: 6
FWCI
1.28
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (Moscow) (publishedVersion)
  • PubMed (publishedVersion)
  • HAL AMU (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
  • Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
Keywords
methionine sulfoxide reductase, methionine sulfoxide, MsrA, MsrB, thiol oxidoreductase, selenocysteine, cysteine, thioredoxin system, protein oxidation, stereospecific reduction, enzyme catalysis, lifespan regulation, stress response
MeSH terms
Amino Acids, Biological Phenomena, Catalysis, Models, Biological, Oxidation-Reduction, Proteins, Catalytic Domain, Methionine Sulfoxide Reductases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review