Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + L-cysteine | Mus musculus | - |
ADP + phosphate + L-glutamyl-L-cysteine | - |
? | |
ATP + L-glutamate + L-cysteine | Homo sapiens | - |
ADP + phosphate + L-glutamyl-L-cysteine | - |
? | |
ATP + L-glutamate + L-cysteine | Rattus norvegicus | - |
ADP + phosphate + L-glutamyl-L-cysteine | - |
? | |
ATP + L-glutamate + L-cysteine | Rattus norvegicus Sprague-Dawley | - |
ADP + phosphate + L-glutamyl-L-cysteine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Rattus norvegicus Sprague-Dawley | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
Hep-G2/C3A cell | - |
Mus musculus | - |
Hep-G2/C3A cell | - |
Homo sapiens | - |
liver | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + L-cysteine | - |
Mus musculus | ADP + phosphate + L-glutamyl-L-cysteine | - |
? | |
ATP + L-glutamate + L-cysteine | - |
Homo sapiens | ADP + phosphate + L-glutamyl-L-cysteine | - |
? | |
ATP + L-glutamate + L-cysteine | - |
Rattus norvegicus | ADP + phosphate + L-glutamyl-L-cysteine | - |
? | |
ATP + L-glutamate + L-cysteine | - |
Rattus norvegicus Sprague-Dawley | ADP + phosphate + L-glutamyl-L-cysteine | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit | Mus musculus |
More | the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit | Homo sapiens |
More | the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
GCL | - |
Mus musculus |
GCL | - |
Homo sapiens |
GCL | - |
Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mus musculus | |
ATP | - |
Homo sapiens | |
ATP | - |
Rattus norvegicus |
Organism | Comment | Expression |
---|---|---|
Homo sapiens | actinomycin D and cycloheximide suppress enzyme expression | down |
Rattus norvegicus | actinomycin D and cycloheximide suppress enzyme expression | down |
Mus musculus | actinomycin D and cycloheximide suppress enzyme expression. 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. Addition of GSH similarly reduces GCLM mRNA abundance | down |
Homo sapiens | catalytic subunit GCLC protein levels do not increase, whereas regulatory subunit GCLM protein levels increase in the cells cultured in cysteine-deficient medium | additional information |
Homo sapiens | both the glutamate-cysteine ligase catalytic (GCLC) and modifier (GCLM) subunit mRNA levels are upregulated in response to a lack of cysteine or other essential amino acids, independent of GSH levels | up |
Rattus norvegicus | both the glutamate-cysteine ligase catalytic (GCLC) and modifier (GCLM) subunit mRNA levels are upregulated in response to a lack of cysteine or other essential amino acids, independent of GSH levels. In liver of rats fed sulfur amino acid-deficient diets, induction of ATF4 and phosphorylation of eIF2alpha are associated with higher levels of GCLC and GCLM mRNA | up |
Mus musculus | both the glutamate-cysteine ligase catalytic (GCLC) and modifier (GCLM) subunit mRNA levels are upregulated in response to a lack of cysteine or other essential amino acids, independent of GSH levels. The upregulation does not occur in MEFs lacking GCN2, i.e. general control non-derepressible 2, also known as eIF2a kinase 4, or in cells expressing mutant eIF2alpha lacking the eIF2alpha kinase Ser51 phosphorylation site, indicating that expression of both GCLC and GCLM is mediated by the GCN2/ATF4 stress response pathway | up |
General Information | Comment | Organism |
---|---|---|
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 | Mus musculus |
physiological function | expression of both glutamate-cysteine ligase catalytic and modifier subunit is mediated by the GCN2/ATF4 stress response pathway. Regulation of modifier subunit GCLM expression may be mediated by changes in the abundance of mRNA stabilizing or destabilizing proteins. Upregulation of GCLM levels in response to low cysteine levels may serve to protect the cell in the face of a future stress requiring GSH as an antioxidant or conjugating/detoxifying agent | Mus musculus |
physiological function | expression of both glutamate-cysteine ligase catalytic and modifier subunit is mediated by the GCN2/ATF4 stress response pathway. Regulation of modifier subunit GCLM expression may be mediated by changes in the abundance of mRNA stabilizing or destabilizing proteins. Upregulation of GCLM levels in response to low cysteine levels may serve to protect the cell in the face of a future stress requiring GSH as an antioxidant or conjugating/detoxifying agent | Homo sapiens |
physiological function | expression of both glutamate-cysteine ligase catalytic and modifier subunit is mediated by the GCN2/ATF4 stress response pathway. Regulation of modifier subunit GCLM expression may be mediated by changes in the abundance of mRNA stabilizing or destabilizing proteins. Upregulation of GCLM levels in response to low cysteine levels may serve to protect the cell in the face of a future stress requiring GSH as an antioxidant or conjugating/detoxifying agent | Rattus norvegicus |