WebGlutaredoxin. Glutaredoxins [1] [2] [3] (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. In humans this oxidation repair enzyme is also known to participate in many cellular functions, including redox signaling and regulation of glucose metabolism. WebDatabase: Pfam Entry: Thioredoxin LinkDB: Thioredoxin Original site: Thioredoxin . All links . Gene (101241) KEGG GENES (101241) Protein sequence (217404) UniProt (216925) …
An Atlas of the Thioredoxin Fold Class Reveals the Complexity of …
WebIn plants, the presence of thioredoxin (Trx), peroxiredoxin (Prx), and sulfiredoxin (Srx) has been reported as a component of a redox system involved in the control of dithiol-disulfide exchanges of target proteins, which modulate redox signalling during development and stress adaptation. Plant thiols, and specifically redox state and ... WebThioredoxin_8. ? Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. ? ? ? pfam13905 is classified as a model that may span more than one domain. pfam13905 is a member of … respawn rsp-900
Identification of thioredoxin genes and analysis of their ... - Springer
WebOther names include thiol specific antioxidant (TSA) and thioredoxin peroxidase (TPx). Mammals express six peroxiredoxins:. 1-Cys ... This article incorporates text from the public domain Pfam and InterPro: IPR000866 This page was last edited on 24 February 2024, at 20:20 (UTC). Text is available under the Creative Commons ... WebJul 30, 2024 · The thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical example thioredoxin and is found in both prokaryotic and eukaryotic proteins. It is an example of an alphabeta protein fold that has oxidoreductase ... Pfam PF00085 InterPro IPR013766 … Webfive protein families is somewhat smaller than thioredoxin itself, having one less 13-strand and one less a-helix. The sequence identity between the five protein classes does not suggest a close structural similarity. ... and thioredoxin (108 residues) are single-domain mono-meric proteins: glutaredoxin has little structure in addi- ... proud fashion bv