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Information on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase
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1.8.4.12 peptide-methionine (R)-S-oxide reductaseIUBMB Comments
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide . While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater . The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well . The enzyme from some species contains selenocysteine and Zn2+.
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Word Map
- 1.8.4.12
- thioredoxins
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selenoproteins
- selenium
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msrbs
- neisseria
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metso
- trx
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sulfenic
- methionine-s-sulfoxide
- meningitidis
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thioredoxin-dependent
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selenoenzyme
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lincosamides
- synthesis
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
hide(3 overall reactions are displayed. Show all (4)>>)
Synonyms
methionine sulfoxide reductase, msrb3, msrb1, msrb2, peptide methionine sulfoxide reductase, msra/b, msrab, cbs-1, methionine-r-sulfoxide reductase, methionine sulfoxide reductase b1, 
more
topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, Cys494 and Cys439 are involved
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, modeling of substrate binding at the active site, Cys444 and Cys495 are involved
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
selenomethionine is essential for MsrB activity
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
the active site selenocysteine SeC169 is essential for enzyme activity
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
three-step catalytic mechanism, influence of pH on reaction mechanism, overview
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L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
proposed catalytic mechanism of the reductase step of MsrB
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism and the role of cofactor recycling in vivo
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism and the role of cofactor recycling in vivo
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism involving residues at positions 95, 41, 97, 77, and 80, molecular modeling, role of selenocysteine- and cysteine residues in catalysis, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism involving residues at positions 95, 41, 97, 77, and 80, molecular modeling, role of selenocysteine- and cysteine residues in catalysis, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
formation of the MsrB substrate complex leads to an activation of the catalytic Cys-117 characterized by a decreased pKapp of about 2.7 pH units. The catalytic active MsrB form is the Cys117-/His103+ species with a pKapp of 6.6 and 8.3, respectively. His103 and to a lesser extent His100, Asn119, and Thr26 (via a water molecule) participate in the stabilization of the polarized form of the sulfoxide function and of the transition state. Trp65 is essential for the catalytic efficiency of the reductase step by optimizing the position of the substrate in the active site
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
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PATHWAY SOURCE
PATHWAYS
BRENDA