Literature summary extracted from
Guo, X.; Song, J.; Guan, T.; Wang, S.; Wang, Y.; Meng, Y.; Guo, J.; Li, T.; Ma, C.; Wei, J.
Characterization of recombinant human gastrointestinal glutathione peroxidase mutant produced in Escherichia coli (2015), Free Radic. Res., 49, 228-235 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.11.1.9 |
expression in Escherichia coli |
Homo sapiens |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.11.1.9 |
molecular modeling of the structure of seleno-hGPx2 |
Homo sapiens |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.11.1.9 |
additional information |
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 |
Homo sapiens |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.11.1.9 |
selenium |
selenium-dependent enzyme |
Homo sapiens |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.11.1.9 |
Homo sapiens |
P18283 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.11.1.9 |
Gpx2 |
- |
Homo sapiens |