Science  People  Locations  Timeline
Index: A B C D E F G H I J K L M N O P Q R S T U V W X Y Z

Home > Glutathione


Glutathione is glutamylcysteinylglycine, a tripeptide. It contains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side chain. Sulfhydryl is kept in a reduced state within ~5 mm in animal cells. In effect, gluathione reduces any disulfide bonds formed within cytoplasmic proteins to cysteines by acting as a buffer.

Glutathione participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidaseThe enzyme glutathione peroxidase ( PDB , EC 1. 9) is a peroxidase found in the erythrocytes of mammals, which helps prevent peroxidation of cell membranes by consuming free peroxide in the cell. The summary reaction the enzyme catalyzes is: : 2GSH + HO &. It is also important as a hydrophilic molecule that is added to lipophilic toxins and waste in the liver during biotransformation before they can become part of the bileBile (or gall is a bitter, greenish-yellow alkaline fluid secreted by the liver of many vertebrates. It is stored in the gallbladder between meals and upon eating is discharged into the duodenum where it aids the process of digestion. Bile salts act to so. Glutathione is also needed for the detoxification of methylglyoxal, a toxin produced as a by-product of metabolism. This detoxification reaction is carried out by the glyoxalase system. Glyoxalase I catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Gluoxalase II catalyzes the conversion of S-D-Lactoyl Glutathione to Reduced Glutathione and D-lactate.

Thiols

Read more »

Non User