EC Number   |
General Information |
Reference |
|---|
    6.3.2.2 | evolution |
Gsh1 belongs to the eu-GC superfamily |
745888 |
| 6.3.2.2 | evolution |
in eukaryotes gamma -glutamylcysteine synthetase and glutathione synthetase, EC 6.3.2.3, activities are encoded by two distinct enzymes In some prokaryotes, such as Escherichia coli and Vibrio cholerae, separate enzymes exist for these two reactions. However, in some prokaryotes, such as Streptococcus agalactiae, Pasteurella multicoda and Listeria monocytogenes, both of these activities are encoded by a single bifunctional enzyme, GshF. Evolution of gamma-GCS has occurred by convergent evolution in three different lineages with no significant sequence similarities between the lineages, the Escherichia coli enzyme belongs to lineage I |
726910 |
| 6.3.2.2 | evolution |
Synechocystis GCL is part of the plant-like GCL family, the Synechocystis enzyme lacks the redox regulation associated with the plant enzymes and functions as a monomeric protein, indicating that evolution of redox regulation occurs later in the green lineage |
726912 |
| 6.3.2.2 | evolution |
the enzyme encoded by GSH1 belongs to the eu-GC superfamily |
745888 |
| 6.3.2.2 | malfunction |
a gene disruptant mutant without GSH1 gene cannot grow in the absence of GSH |
-, 745888 |
| 6.3.2.2 | malfunction |
erythrocytes from gclm-/- mice show greatly reduced intracellular glutathione. Prolonged incubation results in complete lysis of gclm-/- erythrocytes, which can be reversed by exogenous delivery of the antioxidant Trolox. Phenylhydrazine-induced oxidative stress in glcm-/- causes dramatically increased hemolysis, markedly larger accumulations of injured erythrocytes in the spleen, erythrocyte-derived pigment hemosiderin in kidney tubules, and diminished kidney function compared to wild-type mice, phenotype, overview. Regulatory subunit GCLM-deficient erythrocytes are more prone to Ca2+-dependent suicidal cell death ex vivo. Without additional oxidative stress, the mutant animals are able to survive by slightly ramping up their generation of new erythrocytes |
727274 |
| 6.3.2.2 | malfunction |
GSH can be depleted through the specific downregulation of the GCL levels by hammerhead ribozyme |
744469 |
| 6.3.2.2 | malfunction |
in patients with systemic lupus erythematosus (SLE), the levels of enzyme GCL activity and reduced glutathione (GSH) decrease, while thioredoxin (TRX) and oxidized glutathione (GSSG) levels increase when compared with those in the healthy controls. GSH concentrations and GCL activity levels negatively correlate with the SLE disease activity index and erythrocyte sedimentation rate. Patients with SLE and nephritis have lower levels of GSH and GCL activity and higher levels of TRX and GSSG compared with those in SLE patients without nephritis. Insufficient levels of GSH and GCL activity in PBMCs may contribute to the pathogenesis of SLE. A negative association of GSH levels with T-lymphocyte and CD4+ and CD8+ lymphocyte subset apoptosis, and intracellular activated caspase?3 may supports the role of GSH in the alteration of apoptosis of T lymphocytes in the SLE disease state. GSH is involved in the depletion of CD4+ T lymphocytes in patients with SLE |
744853 |
| 6.3.2.2 | malfunction |
overexpression of subunit Gclc-X2 leads to upregulation of the proteins Abcf1, Fkbp4, and Eif3h, as well as to downregulation of protein Lamb1. There is no significant difference in growth rate during exponential phase at 32C between Gclm+ or Gclc-X2+ populations and the wild-type population. A higher cell proliferation observed in the Gclc overexpressing population. Gclc-X2 but not Gclm overexpression increases Gcl activity |
744552 |
| 6.3.2.2 | malfunction |
using GCLC knockout murine embryonic fibroblasts, addition of cysteine to catalytic subunit GCLC null cells results in a marked decrease in regulatory subunit GCLM mRNA levels despite the absence of GSH |
726668 |
