EC Number   |
Protein Variants |
Reference |
|---|
    1.11.1.9 | C2S/C78S/C115S/C156S/C202S |
about 10fold increase in activity compared to wild-type. Mutant displays a typical ping-pong mechanism |
742715 |
| 1.11.1.9 | C74A |
mutation results in a decline of specific activity |
684497 |
| 1.11.1.9 | more |
conversion of the codons for four cysteine residues to the codons for serine residues and change of the codon for Sec40 to the codon for Cys. The recombinant seleno-hGPx2 mutant is obtained using a single protein production system in a cysteine auxotrophic strain, Sec is introduced into the protein via tRNACys misleading. The activity of this mutant is in the same order of magnitude as that of isoform hGPx4, but about one order of magnitude lower than that of hGPx1 and hGPx3. The mutant follows a typical ping-pong mechanism similar to native GPx |
742568 |
| 1.11.1.9 | more |
expression of a recombinant human Gpx3 mutant with all Cys residues changed to Ser from a Cys auxotrophic strain of E. coli. Although lacking post-translational modification, the mutant still retains the ability to reduce H2O2 and 1-palmitoyl-2-(13-hydroperoxy-cis-9, trans-11-octadecadienoyl)-L-3-phosphatidylcholine. Contrary to wild-type, the mutant exists as a monomer in solution |
743791 |
| 1.11.1.9 | more |
full-length (1-201) and C-terminal deletion (1-100) versions of human GPX1 (Sec47Cys), full-length FLAG-GPX1 is modified with O-GlcNAc, while the truncated FLAG-GPX1 is not, despite the fact that truncated GPX1 is still able to bind OGT. O-GlcNAcylation occurs on the C-terminal half of GPX1 |
702092 |
| 1.11.1.9 | more |
GPX1 modified with O-GlcNAc on its C-terminus, cell lysate of VSMCs treated with the O-GlcNAcase inhibitor PUGNAc |
702092 |
| 1.11.1.9 | more |
the enzyme has potential therapeutic value as an antioxidant, but its pharmacological development is limited because the enzyme uses a selenocysteine as its catalytic group and it is difficult to generate selenium-containing proteins with traditional recombinant DNA technology. Rat theta-class glutathione transferase T2-2 (rGST T2-2) presents an ideal scaffold for the design of a novel glutathione peroxidase catalyst because it binds GSH and contains a serine close to substrate binding site, which can be chemically modified to bind selenium. The modified Se-rGST T2-2 efficiently catalyzes the reduction of hydrogen peroxide, and the glutathione peroxidase activity surpasses the activities of some natural glutathione peroxidases |
658429 |
| 1.11.1.9 | N136A |
mutation results in a dramatic decline of specific activity |
684497 |
| 1.11.1.9 | N136D |
mutation results in not detectable specific activity |
684497 |
| 1.11.1.9 | N136H |
mutation results in a dramatic decline of specific activity |
684497 |
