Introduction
The discovery of gludoxin was discovered by Holmgren in 1976 during the redox process of E. coli that lacked the thioredoxin gene, earlier known as "mercaptotransferase". Like thioredoxin, glusaloxin works in a similar way, with an active central disulfide bond. Two cysteine residues in the protein (located in Cys22-Pro-Tyr-CyS25) are linked to each other in the form of intramolecular disulfide bonds, which are either in a reduced state or in an oxidized state.
Glutamoban acts as an electron carrier during glutathione-dependent deoxyribonucleotide synthesis done by the enzyme ribonucleotide reductase. In addition, glutamoban exerts its antioxidant protection effect by reducing dehydroascorbic acid, peroxide oxokisase and methionine sulfoxide reductase. In addition to its function in antioxidant protection, the glutaprosin of bacteria and plants exhibits binding to iron-sulfur clusters and delivering iron-sulfur clusters into enzymes when needed.
virus. Glutamoboxin has been sequenced in multiple species. Based on the homologous fragments, it was preliminarily determined that the O2L protein of vaccinia virus may be gluvoxin. Bacteriophage T4 may be related to evolution. At the fifth position of the T4-type thioredoxin, valine replaces proline.
in plants. Thirty isoforms of glutadoxin were found in the model plant Arabidopsis. Based on their redox active centers, they are classified into three subclasses: CSY[CSs]-, CGSF-, and CC-type. CC-glutamokan is found only in vascular plants. In Arabidopsis, glutamoban is involved in flower development and salicylic acid signaling pathways.
in the human body. In the human body, glutamoxin has an important physiological role. In addition to constituting the antioxidant system, some studies in recent years have shown that the reversible oxidative modification of glutavoxin may be another modification method in addition to phosphorylation, glycosylation and ubiquitination in terms of signal transduction. The modification of this method occurs on the glutadoxin disulfide bond, suggesting the regulation of cellular homeostasis.
The control of bacterial glutamorin on the activity of the transcription factor oxyr has been confirmed, indicating that the response of oxyr to the environment (oxidation state, reduced state) is realized by the glutamide reduction switch. It also plays an important role in anti-apoptosis: glutamokin can bind to apoptosis signal-regulating kinase 1 (ASK1) to inhibit its activity, and when the oxidative state of the cell changes from reduced to oxidized, gluvorexin is released from ASK1 and initiates apoptosis.