1.8.4.11: peptide-methionine (S)-S-oxide reductase

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

Reaction

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

Synonyms

ecdysone-induced protein 28/29 kDa, FMsr, LMJF_07_1140, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase, methionine sulfoxide reductase A, methionine sulfoxide reductases A, methionine sulfoxide-S-reductase, methionine sulphoxide reductase, methionine sulphoxide reductase A, methionine-S-sulfoxide reductase, MetSO-L12 reductase, More, mrsA, MSR, MSR10, MSR180, MsrA, MSRA-1, MsrA/B, MsrA/MsrB, MSRA2, MSRA4, MsrABTk, MsrBA, Peptide Met(O) reductase, peptide methionine S-sulfoxide reductase, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase A, peptide methionine sulfoxide reductase type A, peptide methionine sulphoxide reductase, peptide-methionine (S)-S-oxide reductase, peptide-methionine sulfoxide reductase, PilA, PilB, PilB protein, PMSR, PMSRA, protein-methionine-S-oxide-reductase, sulindac reductase

ECTree

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

Engineering

Engineering on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C15S
monothiol mutant
E55A
almost completely inactive, dimerization is hardly detectable
E55D
almost completely inactive, incapable of dimerization
C15S
-
monothiol mutant
-
E55A
-
almost completely inactive, dimerization is hardly detectable
-
E55D
-
almost completely inactive, incapable of dimerization
-
C151A
-
site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
D134E
-
most active among the mutant enzymes tested, less active than wild-type
D134N
-
lowest activity among all mutants tested for ac-L-Lys-L-Asn-l-Met(O)-L-Asp-L-Lys-dinitrophenol
E99Q
-
lowest activity towards all substrates tested except for ac-L-Lys-L-Asn-l-Met(O)-L-Asp-L-Lys-dinitrophenol
C107S
-
site-directed mutagenesis, the mutant shows 14% increased activity with DTT and 4% with thioredoxin compared to the wild-type enzyme
C107S/C218S
-
site-directed mutagenesis, the mutant shows 78% reduced activity with DTT and 94% with thioredoxin compared to the wild-type enzyme
C107S/C218S/C227S
-
site-directed mutagenesis, the mutant shows 61% reduced activity with DTT and 92% with thioredoxin compared to the wild-type enzyme
C107S/C227S
-
site-directed mutagenesis, the mutant shows 4% reduced activity with DTT and 86% with thioredoxin compared to the wild-type enzyme
C218S
-
site-directed mutagenesis, the mutant shows 65% reduced activity with DTT and 78% with thioredoxin compared to the wild-type enzyme
C218S/C227S
-
site-directed mutagenesis, the mutant shows 58% reduced activity with DTT and 96% with thioredoxin compared to the wild-type enzyme
C227S
-
site-directed mutagenesis, the mutant shows 11% reduced activity with DTT and 81% with thioredoxin compared to the wild-type enzyme
C72S
-
site-directed mutagenesis, inactive mutant, no disulfide bond in the mutant enzyme
C72S/C107S/C227S
-
site-directed mutagenesis, inactuve mutant
C72S/C218S
-
site-directed mutagenesis, inactive mutant
C198S
-
MsrA mutant, mutation of one recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, probably due to formation of a nonproductive complex between sulfenic intermediate and thioredoxin
C86S/C206S
KM and kcat value are 19fold higher and 40fold slower compared to wild type, respectively. The Cys198-Cys206 disulfide bond is rather reduced by thioredoxin under steady-state conditions instead of the Cys51-Cys198 disulfide bond
V231M
mutation to corresponding residue of mouse enzyme, which is hyperoxidized by H2O2. Mutant is sensitive to hyperoxidation
C72A
-
active-site mutant
M229L
mutant is insensitive to hyperoxidation by H2O2
M229V
mutation to corresponding residue of human enzyme, which is not hyperoxidized by H2O2. Mutant is insensitive to hyperoxidation
C198S
C206S
-
site-directed mutagenesis, MsrA domain of PILB, inactive mutant
C348S
-
site-directed mutagenesis, MsrA domain of PILB, mutant is inactive with thioredoxin, but about 10fold more active than the wild-type enzyme MsrA domain
W35F
-
site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme
W53F
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
C25S
-
site-directed mutagenesis, inactive mutant
F26A
-
site-directed mutagenesis, inactive mutant
F26H
-
site-directed mutagenesis, inactive mutant
G24A
-
site-directed mutagenesis, 60% reduced activity compared to the wild-type enzyme
G28A
-
site-directed mutagenesis, 81% reduced activity compared to the wild-type enzyme
W27A
-
site-directed mutagenesis, inactive mutant
C180S
C188S
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C194S
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C285S
kcat value is similar to that of wild-type, while its Km value is slightly higher than that of the wild type
D164A
catalytic efficiency is about 120% of wild-type
E165A
catalytic efficiency is similar to wild-type
Y163A
catalytic efficiency is about 60% of wild-type
Y163A/E165A
catalytic efficiency is about 8% of wild-type
additional information