Literature summary for 1.11.1.27 extracted from

Wang, L.L.; Lu, S.Y.; Hu, P.; Fu, B.Q.; Li, Y.S.; Zhai, F.F.; Ju, D.D.; Zhang, S.J.; Su, B.; Zhou, Y.; Liu, Z.S.; Ren, H.L.
Construction and activity analyses of single functional mouse peroxiredoxin 6 (Prdx6) (2019), J. Vet. Res., 63, 99-105 .

Search for more literature for 1.11.1.27

Protein Variants

Protein Variants	Comment	Organism
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	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	O08709	bifunctional protein with glutathione peroxidase activity and phospholipase A2 activity	-

Synonyms

Synonyms	Comment	Organism
peroxiredoxin 6	-	Mus musculus
Prdx6	cf. EC 3.1.1.4	Mus musculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)