Crystallization (Comment) | Organism |
---|---|
the crystal structure of the loopless mutant, in which the loop is replaced by 3 Gly residues, is identical with that of the wild-type enzyme | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the crystal structure of the loopless mutant, in which the loop is replaced by 3 Gly residues, is identical with that of the wild-type enzyme. Replacement of the loop increases the Km-values, especially for glycine, and a 930fold decrease in turnover number. The loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | loopless mutant with increased Km-values, especially for Gly | Escherichia coli | |
0.24 | - |
ATP | gamma-Glu-Cys, wild-type enzyme | Escherichia coli | |
0.7 | - |
gamma-Glu-Cys | loopless mutant | Escherichia coli | |
0.91 | - |
Gly | wild-type enzyme | Escherichia coli | |
1.54 | - |
ATP | loopless mutant | Escherichia coli | |
29.8 | - |
Gly | loopless mutant | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
B | - |
Escherichia coli | - |
wild-type and loopless mutant, in which the loop (Ile226-Arg241) is replaced with 3 Gly residues | - |
Escherichia coli B / ATCC 11303 | - |
B | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione | the catalytic mechanism is proposed to proceed via phosphorylation of the dipeptide substrate to yield an acyl phosphate intermediate. This intermediate is subsequently attacked by glycine, followed by loss of inorganic phosphate, leading to glutathione formation | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + gamma-Glu-L-Cys + Gly | - |
Escherichia coli | ADP + phosphate + glutathione | - |
? | |
ATP + gamma-Glu-L-Cys + Gly | - |
Escherichia coli B / ATCC 11303 | ADP + phosphate + glutathione | - |
? | |
additional information | the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity | Escherichia coli | ? | - |
? | |
additional information | the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity | Escherichia coli B / ATCC 11303 | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | loopless mutant with a 930fold decrease in turnover number | Escherichia coli |