نتایج جستجو برای: methionine sulfoxide reductase

تعداد نتایج: 70481  

2011
Luisa A. Denkel Sarah A. Horst Syed Fazle Rouf Vera Kitowski Oliver M. Böhm Mikael Rhen Timo Jäger Franz-Christoph Bange

Production of reactive oxygen species represents a fundamental innate defense against microbes in a diversity of host organisms. Oxidative stress, amongst others, converts peptidyl and free methionine to a mixture of methionine-S- (Met-S-SO) and methionine-R-sulfoxides (Met-R-SO). To cope with such oxidative damage, methionine sulfoxide reductases MsrA and MsrB are known to reduce MetSOs, the f...

Journal: :Plant physiology 1992
D L Ferguson J J Burke

A new assay for measuring protein-methionine-S-oxide reductase is reported. The assay measures the conversion of N-(9-fluorenylmethoxycarbonyl)-methionine sulfoxide to N-(9-fluorenylmethoxycarbonyl)-methionine using fluorescence detection after high-performance liquid chromatography separation. Enzyme activity is linear over a 60-min period and the assay is sensitive enough to detect the consum...

Journal: :Molecules 2009
Derek B Oien Jackob Moskovitz

Selenium is a chemical element participating in the synthesis of selenocysteine residues that play a pivotal role in the enzymatic activity efficiency of selenoproteines. The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, resp...

Journal: :BMB reports 2011
Yongjoon Kim Geun-Hee Kwak Chuhee Lee Hwa-Young Kim

Human methionine sulfoxide reductase B3A (hMsrB3A) is an endoplasmic reticulum (ER) reductase that catalyzes the stereospecific reduction of methionine-R-sulfoxide to methionine in proteins. In this work, we identified an antimicrobial peptide from hMsrB3A protein. The N-terminal ER-targeting signal peptide (amino acids 1-31) conferred an antimicrobial effect in Escherichia coli cells. Sequence...

Journal: :Journal of bacteriology 1998
C S Hayes B Illades-Aguiar L Casillas-Martinez P Setlow

Methionine residues in alpha/beta-type small, acid-soluble spore proteins (SASP) of Bacillus species were readily oxidized to methionine sulfoxide in vitro by t-butyl hydroperoxide (tBHP) or hydrogen peroxide (H2O2). These oxidized alpha/beta-type SASP no longer bound to DNA effectively, but DNA binding protected alpha/beta-type SASP against methionine oxidation by peroxides in vitro. Incubatio...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2001
J Moskovitz S Bar-Noy W M Williams J Requena B S Berlett E R Stadtman

Oxidation of proteins by reactive oxygen species is associated with aging, oxidative stress, and many diseases. Although free and protein-bound methionine residues are particularly sensitive to oxidation to methionine sulfoxide derivatives, these oxidations are readily repaired by the action of methionine sulfoxide reductase (MsrA). To gain a better understanding of the biological roles of MsrA...

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