Protein Variants | Comment | Organism |
---|---|---|
C248A/C249A | mutant enzyme shows the same strength of binding to regulatory subunit (GCLM) as does wild-type GCLC, yet the catalytic activity is dramatically decreased | Mus musculus |
additional information | deletion analysis indicats that most regions, except a portion of the C-terminal region of catalytic subunit (GCLC) and a portion of the N-terminal region of regulatory subunit (GCLM), are required for the interaction to occur | Mus musculus |
P158L | mutant enzyme shows the same strength of binding to regulatory subunit (GCLM) as does wild-type GCLC, yet the catalytic activity is dramatically decreased | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
GSH | - |
Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + L-cysteine | Mus musculus | rate-limiting enzyme in the glutathione biosynthesis pathway | ADP + phosphate + gamma-L-glutamyl-L-cysteine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + L-cysteine | rate-limiting enzyme in the glutathione biosynthesis pathway | Mus musculus | ADP + phosphate + gamma-L-glutamyl-L-cysteine | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | heterodimer, comprising a catalytic subunit (GCLC) and a regulatory subunit (GCLM). GCLC alone can catalyze the formation of L-gamma-glutamyl-L-cysteine, its binding with GCLM enhances the enzyme activity by lowering the Km for glutamate and ATP, and increasing the Ki for GSH inhibition | Mus musculus |