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Results 1 - 10 of 10
EC Number
Inhibitors
Commentary
Structure
3-carboxy 4-nitrobenzenethiol
binds specifically to the sulfenic acid reaction intermediate
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dimedone
binds specifically to the sulfenic acid reaction intermediate
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dimethyl sulfoxide
DMSO competitively inhibits the methionine-sulfoxide reduction ability of MsrA (12% residual activity at 0.1% (v/v) DMSO) and inhibits the antioxidant function of MsrA in yeast cells, resulting in higher sensitivity to oxidative stress
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H2O2
1 mM, 85% deactivation. The active site of this enzyme is significantly altered after H2O2-mediated oxidation of L-methionine, L-tryptophan, and L-cysteine residues in its active site
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H2O2
the enzyme is only inactivated by high doses of H2O2, when treated with 0.5 mM H2O2 MsrA loses 20% of its activity and this inhibition reaches approximately 40% with 1 mM H2O2, MsrA is not significantly inhibited by lower concentrations of H2O2 (0.050 and 0.1 mM)
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H2O2
in the mouse enzyme, the sulfenic acid formed at the catalytic Cys residue is vulnerable to irreversible oxidation to cysteine sulfinic acid resulting in inactivation. Hyperoxidation is controlled by the presence or absence of residue Met229 in the carboxyl terminal domain. Mouse msrA becomes insensitive to hyperoxidation when the Met229 is mutated. Hyperoxidation occurs so long as the methionine is located within the 14 carboxyl terminal residues. Met229 may form a stable, non-covalent bond with Trp74 at the active site, preventing formation of a protective sulfenylamide with Cys72 sulfenic acid
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effects of high light, ozone, and paraquat on enzyme activity and photosynthetic activity in wild-type and transgenic plants, overview
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enzyme expression decreases during dehardening from 4C to 22C of cold-acclimated plants, effects of light and temperature on enzyme expression and activity, overview
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isozyme PMSRA5 expression is slightly suppressed by ozone
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contrary to the mouse enzmye, human MsrA is not sensitive to hyperoxidation by H2O2
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Results 1 - 10 of 10