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
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1.8.98.2
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peroxiredoxins
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hyperoxidation
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thioredoxins
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overoxidized
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sulfenic
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peroxidatic
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txnrd1
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sulfinylated
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deglutathionylation
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prxiii
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prdxs
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cys-so2h
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medicine
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drug development
- 1.8.98.2
- peroxiredoxins
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hyperoxidation
- thioredoxins
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overoxidized
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sulfenic
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peroxidatic
- txnrd1
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sulfinylated
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deglutathionylation
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prxiii
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prdxs
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cys-so2h
- medicine
- drug development
Reaction
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
1.8.98.2 sulfiredoxinAdvanced search results
results (
results (Results
in table
1
1793
17
50
26
54
Engineering
Engineering on EC 1.8.98.2 - sulfiredoxin
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C72S
E76A
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
K40Q
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site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R28Q
R28Q/E76A
C72S
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site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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E76A
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
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R28Q
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site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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C99A
C99S
C106A
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mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A
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mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A/C106A
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mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C84S
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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
C72S
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site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
C72S
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loss of sulfinate reductase activity, no effect on DNA binding and hydrolizing activities
C72S
site-directed mutagenesis, the cysteine-deficient mutation at the active completely abolishes activity of Srx
R28Q
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site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R28Q
site-directed mutagenesis, the mutation in AtSrx only partially reduces its activity and needs the additional mutation of E76 to totally inactivation. The survived activity of AtSrx may be the result of that AtSrx has two more arginine residues at the loop next to alpha1. The side chains of Arg32 and Arg34, which can swing to the side of Cys72, may partially compensate for the effects of the loss of Arg28
R28Q/E76A
site-directed mutagenesis, the double mutation disrupts the stability of the loop in which Arg32/Arg34 is located, therefore AtSrx is completely inactivated
C99A
site-directed mutagenesis, the mutation leads to a complete loss of both Srx enzymatic activity and binding to substrates such as Prxs
C99S
mutant created to show the importance of the cytosine residue in the deglutathionylation function of the protein
additional information
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construction of a Srx knockout mutant, phenotype, overview
additional information
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construction of a Srx knockout mutant, phenotype, overview
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additional information
several lentiviral shRNAs targeting separate coding regions of Srx mRNA (shSrx) are used to knockdown the levels of endogenously expressed protein. Two shRNAs targeting the coding regions of TXNDC5 have the highest efficiency to inhibit the expression of endogenous protein. These shRNAs are introduced into A549 and H226 cells by viral infection. Enzyme knockdown in in stable A-549 or H-226 cells expressing shSrx1 or shSrx2. Knockdown of Srx leads to a rapid activation of the unfolded protein response (UPR) and sensitizes human lung cancer cells to ER stress-induced cell death
additional information
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several lentiviral shRNAs targeting separate coding regions of Srx mRNA (shSrx) are used to knockdown the levels of endogenously expressed protein. Two shRNAs targeting the coding regions of TXNDC5 have the highest efficiency to inhibit the expression of endogenous protein. These shRNAs are introduced into A549 and H226 cells by viral infection. Enzyme knockdown in in stable A-549 or H-226 cells expressing shSrx1 or shSrx2. Knockdown of Srx leads to a rapid activation of the unfolded protein response (UPR) and sensitizes human lung cancer cells to ER stress-induced cell death
additional information
Srx mutant variants analyzed by circular dichroism spectroscopy (JASCO-720) in 20 mM HEPES, pH 7.5, 100 mM NaCl at a concentration from 0.4 mg/ml are confirmed to exhibit wild-type-like spectra
additional information
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Srx mutant variants analyzed by circular dichroism spectroscopy (JASCO-720) in 20 mM HEPES, pH 7.5, 100 mM NaCl at a concentration from 0.4 mg/ml are confirmed to exhibit wild-type-like spectra
