Literature summary for 1.11.1.9 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 .

Search for more literature for 1.11.1.9

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular modeling of the structure of seleno-hGPx2	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
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

Metals/Ions	Comment	Organism	Structure
selenium	selenium-dependent enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P18283	-	-

Synonyms

Synonyms	Comment	Organism
Gpx2	-	Homo sapiens

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Release 2023.1 (January 2023)