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1.11.1.27: glutathione-dependent peroxiredoxin

This is an abbreviated version!
For detailed information about glutathione-dependent peroxiredoxin, go to the full flat file.

Word Map on EC 1.11.1.27

Reaction

2 glutathione +

ROOH
=
glutathione disulfide
+
H2O
+
ROH

Synonyms

1-Cys peroxiredoxin, 1-Cys Prdx, 1-Cys Prx, 1-CysPrx, 2-Cys peroxiredoxin, 2-Cys peroxiredoxin TPx-1, EC 1.11.1.15, glutathione peroxidase, GPX, HI0572, peroxiredoxin 6, peroxiredoxin II, peroxiredoxin VI, Pf1-Cys-Prx, PGdx, Prdx6, Prx1, Prx3, Prx6, TPx-1

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.27 glutathione-dependent peroxiredoxin

Engineering

Engineering on EC 1.11.1.27 - glutathione-dependent peroxiredoxin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C47S
mutation abolishes peroxidase activity,mutation has no effect on lipase activity
C91S
mutation has no effect on lipase activity
S32A
mutation has no effect on lipase activity
S32G
mutation has no effect on lipase activity
C185S
-
inactive mutant enzyme
D140A
mutant shows decreased peroxidase activity
H26A
mutant shows decreased peroxidase activity
S32A
mutant shows decreased peroxidase activity with H2O2 and no activity with 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate
additional information
peroxiredoxin 6 is a bifunctional protein with glutathione peroxidase activity and phospholipase A2 activity. A Prdx6 enzyme with a single activity is constructed to facilitate study of the relationship between the single function of Prdx6 and Brucella infection. The target open reading frame DNAs of Prdx6 with a single active centre are prepared using gene splicing by overlap extension PCR, and the recombinant eukaryotic expression plasmids inserted by Prdx6 with the single activity centre are constructed and transfected into murine Raw264.7 macrophages. The glutathione peroxidase activity and phospholipase A2 activity of the constructed Prdx6 are examined. The core centres (Ser32 and Cys47) of Prdx6 are successfully mutated by changing the 94th nucleotide from T to G and the 140th nucleotide from G to C in the two enzyme activity cores, respectively. The constructed recombinant plasmids of Prdx6 with the single active centre are transfected into murine macrophages showing the expected single functional enzyme activity, which MJ33 or mercaptosuccinate inhibitors are able to inhibit