Literature summary extracted from
Pai, C.H.; Wu, H.J.; Lin, C.H.; Wang, A.H.
Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases (2011), Protein Sci., 20, 557-566.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.5.1.78 |
mutant enzyme C59A is expressed in Escherichia coli BL21(DE3) cells |
Escherichia coli |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.5.1.78 |
mutant enzyme C59A in complex with glutathionylspermidine |
Escherichia coli |
6.3.1.8 |
mutant C59A lacking amidase activity, in complex with amidase substrate gluthionylspermidine and ADP. Homodimer, and each monomer contains the N-terminal amidase and C-terminal synthetase domains connected by a linker in between |
Escherichia coli |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.5.1.78 |
C59A |
active site mutant |
Escherichia coli |
Natural Substrates/ Products (Substrates)
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 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.1.78 |
Escherichia coli |
P0AES0 |
bifunctional enzyme glutathionylspermidine synthetase/amidase |
- |
6.3.1.8 |
Escherichia coli |
P0AES0 |
bifunctional glutathionylspermidine synthetase/amidase |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.5.1.78 |
nickel affinity column chromatography |
Escherichia coli |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.5.1.78 |
glutathionylspermidine + H2O |
- |
Escherichia coli |
glutathione + spermidine |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.5.1.78 |
Glutathionylspermidine synthetase/amidase |
bifunctional enzyme |
Escherichia coli |
3.5.1.78 |
GSP amidase |
- |
Escherichia coli |
3.5.1.78 |
GspA |
glutathionylspermidine amidase domain of GspSA |
Escherichia coli |
3.5.1.78 |
GspSA |
bifunctional enzyme |
Escherichia coli |