1.8.98.2: sulfiredoxin

This is an abbreviated version!
For detailed information about sulfiredoxin, go to the full flat file.

Word Map on EC 1.8.98.2

Reaction

peroxiredoxin-(S-hydroxy-S-oxocysteine)
+
ATP
+ 2 R-SH =
peroxiredoxin-(S-hydroxycysteine)
+
ADP
+
phosphate
+
R-S-S-R

Synonyms

AtSrx, cysteine-sulfinic acid reductase, neoplastic progression 3, peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase, protein cysteine sulfinic acid reductase, Srx, Srx1, Srxn1, sulfiredoxin, sulfiredoxin 1, sulfiredoxin-1, sulphiredoxin

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.98 With other, known, physiological acceptors
                1.8.98.2 sulfiredoxin

Engineering

Engineering on EC 1.8.98.2 - sulfiredoxin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E76A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
K40Q
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R28Q
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R28Q/E76A
-
site-directed mutagenesis, inactive mutant
C72S
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
E76A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
R28Q
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
R28Q/E76A
-
site-directed mutagenesis, inactive mutant
-
C99A
-
Cys99 replaced by Ala
D57N
-
Asp57 replaced by Asn
D79N
-
Asp60 replaced by Asn
H100N
-
Srx mutant
H99N
-
His99 replaced by Asn
K60R
-
Lys60 replaced by Arg
R100M
-
Arg100 replaced by Met
R101M
-
Srx mutant
R50M
-
Arg50 replaced by Met
Y92R
-
Srx mutant
C106A
-
mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A
-
mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A/C106A
-
mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C84S
-
Srx1 reactivates the yeast Prx1 peroxidase activity that is inactivated by H2O2. Mutant C84S does not induce the reactivation of inactivated Prx1 or dissociation of the high molecular weight Prx1 complex
additional information