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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 .
    View publication on PubMed

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
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-

Synonyms

EC Number Synonyms Comment Organism
1.11.1.9 Gpx2
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Homo sapiens