ArticleProtein science : a publication of the Protein Society2001
E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 47 citations in OpenAlex.
- Oxidative stress, protein damage and repair in bacteria.Nature reviews. Microbiology · 2017Review
- A Kinetic Platform to Determine the Fate of Hydrogen Peroxide in Escherichia coli.PLoS computational biology · 2015Article
- Corynebacterium glutamicum methionine sulfoxide reductase A uses both mycoredoxin and thioredoxin for regeneration and oxidative stress resistance.Applied and environmental microbiology · 2015Article
- Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii.PloS one · 2015Article
- Genes required for alleviation of uranium toxicity in sulfate reducing bacterium Desulfovibrio alaskensis G20 [corrected].Ecotoxicology (London, England) · 2014Article
- Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding.The Journal of biological chemistry · 2012Article
- The logic of kinetic regulation in the thioredoxin system.BMC systems biology · 2011Article
- Functional genetic diversity among Mycobacterium tuberculosis complex clinical isolates: delineation of conserved core and lineage-specific transcriptomes during intracellular survival.PLoS pathogens · 2010Article
- Thioredoxin is involved in U(VI) and Cr(VI) reduction in Desulfovibrio desulfuricans G20.Journal of bacteriology · 2009Article
- Mycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochlorite.Molecular microbiology · 2009Article
- The role of prophage for genome diversification within a clonal lineage of Lactobacillus johnsonii: characterization of the defective prophage LJ771.Journal of bacteriology · 2008Article
- Increased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensis.Biochemistry · 2007Article
- Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The glutathione-glutaredoxin system in Rhodobacter capsulatus: part of a complex regulatory network controlling defense against oxidative stress.Journal of bacteriology · 2004Article
- Arabidopsis peptide methionine sulfoxide reductase2 prevents cellular oxidative damage in long nights.The Plant cell · 2004Article
- Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.Journal of bacteriology · 2003Article
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3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The monomeric peptide methionine sulfoxide reductase (MsrA) catalyzes the irreversible thioredoxin-dependent reduction of methionine sulfoxide. The crystal structure of MsrAs from Escherichia coli and Bos taurus can be described as a central core of about 140 amino acids that contains the active site. The core is wrapped by two long N- and C-terminal extended chains. The catalytic mechanism of the E. coli enzyme has been recently postulated to take place through formation of a sulfenic acid intermediate, followed by reduction of the intermediate via intrathiol-disulfide exchanges and thioredoxin oxidation. In the present work, truncated MsrAs at the N- or C-terminal end or at both were produced as folded entities. All forms are able to reduce methionine sulfoxide in the presence of dithiothreitol. However, only the N-terminal truncated form, which possesses the two cysteines located at the C-terminus, reduces the sulfenic acid intermediate in a thioredoxin-dependent manner. The wild type displays a ping-pong mechanism with either thioredoxin or dithiothreitol as reductant. Kinetic saturation is only observed with thioredoxin with a low K(M) value of 10 microM. Thus, thioredoxin is likely the reductant in vivo. Truncations do not significantly modify the kinetic properties, except for the double truncated form, which displays a 17-fold decrease in k(cat)/K(MetSO). Alternative mechanisms for sulfenic acid reduction are also presented based on analysis of available MsrA sequences.
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