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Literature summary for 6.3.2.2 extracted from
- Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase (2009), J. Biol. Chem., 284, 32700-32708.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| homology model of the catalytic subunit of human glutamate cysteine ligase. Examination of the model suggests that post-translational modifications of cysteine residues may be involved in the regulation of enzymatic activity | Homo sapiens |
| structures of glutamate cysteine ligase in the presence of glutamate and MgCl2, to 2.1 A resolution, and in complex with glutamate, MgCl2, and ADP to 2.7 A resolution. Structures reveal an unusual binding pocket for the alpha-carboxylate of the glutamate substrate and an ATP-independent Mg2+ coordination site, clarifying the Mg2+-dependence of the enzymatic reaction | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Saccharomyces cerevisiae | P32477 | - |
- |
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Release 2023.1 (January 2023)
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