EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.78 | additional information | site-directed mutagenesis indicates that Cys59 is essential for amidase activity | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.78 | iodoacetamide | - |
Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.78 | additional information | - |
additional information | - |
Escherichia coli | |
3.5.1.78 | 5.5 | - |
glutathionylspermidine | C173A mutant amidase fragment | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.78 | glutathionylspermidine + H2O | Escherichia coli | - |
glutathione + spermidine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.78 | Escherichia coli | - |
bifunctional enzyme glutathionylspermidine synthetase/amidase | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.5.1.78 | glutathionylspermidine + H2O = glutathione + spermidine | evidence for a glutathionyl-enzyme intermediate in the amidase activity of the bifunctional enzyme | Escherichia coli | |
3.5.1.78 | glutathionylspermidine + H2O = glutathione + spermidine | glutathionylspermidine + H2O = glutathione + spermidine, , nucleophilic attack mechanism involving Cys as the catalytic nucleophile | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.78 | gamma-Glu-Ala-Gly-4-nitroanilide + H2O | - |
Escherichia coli | ? | - |
? | |
3.5.1.78 | glutathionylspermidine + H2O | - |
Escherichia coli | glutathione + spermidine | - |
? |