2008
DOI: 10.1016/j.abb.2008.02.007
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The methionine sulfoxide reductases: Catalysis and substrate specificities

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Cited by 163 publications
(161 citation statements)
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“…For WT MSRB1, the calculations revealed that only ϳ0.5 Cys-SOH was titrated per mol of oxidized MSRB (Fig. 5), a value twice lower than that expected regarding the catalytic mechanism used by MSRBs (21,50). Similarly, ϳ0.5 Cys-SOH, instead of a value of 1, was recorded for the mutated poplar MSRA possessing only the catalytic Cys.…”
Section: Reductantmentioning
confidence: 90%
“…For WT MSRB1, the calculations revealed that only ϳ0.5 Cys-SOH was titrated per mol of oxidized MSRB (Fig. 5), a value twice lower than that expected regarding the catalytic mechanism used by MSRBs (21,50). Similarly, ϳ0.5 Cys-SOH, instead of a value of 1, was recorded for the mutated poplar MSRA possessing only the catalytic Cys.…”
Section: Reductantmentioning
confidence: 90%
“…Despite the fact that the three families have distinct differences in origin, structure, substrate specificity, and species distribution, they basically share a similar catalytic mechanism. The mechanism involves the oxidation of the catalytic cysteine to a sulfenic acid intermediate, followed by the formation of an intramolecular disulfide bond, and the final regeneration process driven by Trx or other reductants (6,7,(15)(16)(17)(18).…”
Section: Thioredoxins (Trxs)mentioning
confidence: 99%
“…In addition to MsrA and MsrB functions, previous studies suggested the presence of additional Msr activities in Escherichia coli and yeast cells, which were especially evident in cells deficient in both enzymes (14,(21)(22)(23). Recently, Lowther and colleagues (24) discovered a new enzyme, designated fRMsr (free Met-R-SO reductase), which catalyzes the reduction of free Met-R-SO in E. coli.…”
mentioning
confidence: 99%