Crystallization (Comment) | Organism |
---|---|
crystallization by vapour-diffusion hanging-drop method of the free enzyme or the enzyme liganded to substrate gamma-glutamylcysteine and non-hydrolyzable ATP-substrate-analogue AMP-PNP, 17 mg/ml enzyme in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, plus equal volume of reservoir solution: for crystals of free enzyme with 1.97 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400 at 22°C, or for the liganded enzyme with 3 mM AMP-PNP, 10 mM MgCl2, 3 mM gamma-glutamylcysteine against a well solution of 2.2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400, 5 mM TCEP, 40 mM MgCl2, at 22°C, X-ray diffraction structure determination and analysis at 2.3 A and 1.8 A, respectively | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, binding structure | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + gamma-L-Glu-L-Cys + Gly | Saccharomyces cerevisiae | final step in glutathione biosynthesis | ADP + phosphate + glutathione | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q08220 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione | determination of reaction and substrate binding mechanisms, large conformational changes in the catalytic cycle | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + gamma-L-Glu-L-Cys + Gly | - |
Saccharomyces cerevisiae | ADP + phosphate + glutathione | - |
ir | |
ATP + gamma-L-Glu-L-Cys + Gly | final step in glutathione biosynthesis | Saccharomyces cerevisiae | ADP + phosphate + glutathione | - |
ir |
Subunits | Comment | Organism |
---|---|---|
dimer | homodimer, crystal structure | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
GS | - |
Saccharomyces cerevisiae |
More | enzyme belongs to the ATP-grasp enzyme superfamily | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on, binding structure | Saccharomyces cerevisiae |