Glutathione amide reductase information

Glutathione amide reductase (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This enzyme catalyses the following...

GSH synthesis. The unusual gamma amide linkage in glutathione protects it from hydrolysis by peptidases. Glutathione is the most abundant non-protein...

has to be broken, In human cells, this is done by glutathione reductase(GR). Glutathione reductase is a dimer that contains two identical subunits. It...

enzymes, glutathione reductase (GR) and thioredoxin reductase (Trx1), and two mitochondrial enzymes, lipoamide dehydrogenase and thioredoxin reductase (Trx2)...

catalysed by ribonucleotide reductase (see figure). Thiyl intermediates also are produced by the oxidation of glutathione, an antioxidant in biology....

Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a class III alcohol...

environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple". Free Radic Biol Med. 30 (11): 1191–212. doi:10...

formation between proline and other amino acids. When proline is bound as an amide in a peptide bond, its nitrogen is not bound to any hydrogen, meaning it...

the side chain's extra methyl group such proteases use their N-terminal amide as the base, rather than a separate amino acid. Use of oxygen or sulfur...

the kidney. It is broken down by the enzyme, protein-disulfide reductase (glutathione), which breaks the disulphide bonds between the A and B chains....

contain selenols at their active sites: glutathione peroxidase, iodothyronine deiodinase, and thioredoxin reductase. The selenols in these proteins are part...

substrates are negatively charged natural compounds or drugs modified by glutathione, conjugation, glycosylation, sulfation and glucuronylation. Drugs can...