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1.8.4.12: peptide-methionine (R)-S-oxide reductase

This is an abbreviated version!
For detailed information about peptide-methionine (R)-S-oxide reductase, go to the full flat file.

Word Map on EC 1.8.4.12

Reaction

L-methionine (R)-sulfoxide
+
thioredoxin
=
L-methionine
 +
thioredoxin disulfide
 +
H2O

Synonyms

1-Cys methionine sulfoxide reductase B, 1-Cys MSRB, CBS-1, CBS1, cysteine-containing methionine-R-sulfoxide reductase, LOC100305558, LOC100798757, methionine sulfoxide reductase, methionine sulfoxide reductase B, methionine sulfoxide reductase B1, methionine sulfoxide reductase B2, methionine sulfoxide reductase B3, methionine sulfoxide reductase B8, methionine sulfoxide reductase MsrB3, methionine sulfoxide reductases B, methionine sulfoxide reductases B2, methionine sulphoxide reductase, methionine-R-sulfoxide reductase, methionine-R-sulfoxide reductase B, methionine-R-sulfoxide reductase B2, MetO reductase, More, MSR, MsrA, MsrA/B, MsrA/MsrB, msrAB, MsrABTk, MsrB, MSRB1, MsrB2, MsrB3, MsrB3A, MSRB4, MsrB5, MsrB7, MsrB8, MsrBA, Mxr2, NtMsrB2, OsMSRB5, PaMsrB1, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase type B, PilB, PilB protein, PMSR, Sel-X, selenocysteine-containing methionine-R-sulfoxide reductase, selenoprotein R, SelR, sulindac reductase, TbmsrB, TCDM_06423, YeaA

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.12 peptide-methionine (R)-S-oxide reductase

Engineering

Engineering on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C116S
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
C134T
-
MSRB2 mutant with increased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
C151A
-
site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
T132A
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
T132C
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
C45D/C48S/C94S/C97S
-
site-directed mutagenesis, the mutant MsrB loses binding ability for Zn2+ and Fe2+, and shows no catalytic activity in presence of thioredoxin or DTT, substitution of the two cysteine residues of MsrB results in complete loss of the enzyme's metal binding and reductase activity
C121S
-
the mutant of isoform MSRB2 is inactive
C68S
-
the mutant of isoform MSRB2 is inactive
D197A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 2.6fold lower than wild-type value
E193A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 2.4fold lower than wild-type value
E193A/D197A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 3.1fold lower than wild-type value
E339A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 1.39fold lower than wild-type value
Y343F
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 1.1fold lower than wild-type value
D197A
-
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 2.6fold lower than wild-type value
-
E193A
-
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 2.4fold lower than wild-type value
-
E193A/D197A
-
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 3.1fold lower than wild-type value
-
E339A
-
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 1.39fold lower than wild-type value
-
Y343F
-
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 1.1fold lower than wild-type value
-
C105S
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
C169S
-
site-directed mutagenesis, active site mutant, completely inactive mutant
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to highly reduced activity with cofactor thioredoxin or DTT compared to wild-type MsrB3
H77G/I81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
H77G/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
I81E
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to slightly increased activity with cofactor thioredoxin and reduced activcity with DTT compared to wild-type MsrB3
N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB3
N97Y
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant shows highly reduced activity with cofactor DTT or thioredoxin compared to wild-type MsrB3
W110A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C98S
the mutant show increased Km values with dithiothreitol (1.7fold) and thioredoxin (6fold) compared to the wild type enzyme
E81V
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB1s
F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, the selenocysteine-containing mutant shows reduced activity with either cofactor thioredoxin and DTT compared to wild-type selenocysteine MsrB1, while the cysteine-containing mutant shows activity and kinetics similar to the wild-type cysteine MsrB1
G77H/E81V/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to highly reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
H77G/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
H77G/V81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB2
N97Y
-
site-directed mutagenesis, mutation of isozyme MsrB2, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB2
U95C
the mutant has a significantly decreased activity
V81E
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
L38M/L41M
-
site-directed mutagenesis, mutation of the NT domain of PilB, thioredoxin binding structure, crystal structure analysis, overview
C439S
-
site-directed mutagenesis, MsrA domain of PILB, mutant is inactive with thioredoxin, but about 10fold more active than the wild-type enzyme MsrA domain
C494S
-
site-directed mutagenesis, MsrA domain of PILB, inactive mutant
C63S
-
site-directed mutagenesis, the mutant accumulates the sulfenic acid intermediate, while the wild-type accumulates the disulfide intermediate
D45C/S48C/S94C/A97C
-
site-directed mutagenesis, the mutant MsrB shows increased binding of Zn2+ and Fe2+ compared to the wild-type enzyme, overview, introduction of two cysteine residues into Neisseria meningitidis MsrB analogously to the Escherichia coli enzyme results in increased tight binding of zinc to and strongly increased thermal stability with wild-type reductase activity but no thioredoxin recycling activity
W65F
-
site-directed mutagenesis, structural change of substrate binding and active site structure compared to the wild-type enzyme
C181S
-
inactive
C11S
catalytic efficiency is about 140% of wild-type
D164A
catalytic efficiency is about 80% of wild-type
E165A
catalytic efficiency is about 65% to wild-type
Y163A
catalytic efficiency is about 20% of wild-type
Y163A/E165A
catalytic efficiency is about 17% of wild-type
C11S
-
catalytic efficiency is about 140% of wild-type
-
D164A
-
catalytic efficiency is about 80% of wild-type
-
E165A
-
catalytic efficiency is about 65% to wild-type
-
Y163A
-
catalytic efficiency is about 20% of wild-type
-
Y163A/E165A
-
catalytic efficiency is about 17% of wild-type
-
C128S
inactive mutant enzyme
C72S
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 7fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
C72S/C74S
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. The mutant enzyme is unable to use Trypanosoma cruzi tryparedoxin or Trypanosoma cruzi thioredoxin as reducing substrates, being able to use trypanothione disulfide as a direct reducing substrate. The double mutation allows the protein to use glutathione as a reductant
C74S
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 2fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
C128S
-
inactive mutant enzyme
-
C72S
-
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 7fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
-
C72S/C74S
-
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. The mutant enzyme is unable to use Trypanosoma cruzi tryparedoxin or Trypanosoma cruzi thioredoxin as reducing substrates, being able to use trypanothione disulfide as a direct reducing substrate. The double mutation allows the protein to use glutathione as a reductant
-
C74S
-
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 2fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
-
additional information