CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1720 | endopeptidase fold (from Nostoc punctiforme) |
|
3.90.1720.10 | endopeptidase domain like (from Nostoc punctiforme) |
Domain Context
CATH Clusters
| Superfamily | endopeptidase domain like (from Nostoc punctiforme) |
| Functional Family | Bifunctional glutathionylspermidine synthetase/amidase |
Enzyme Information
| 3.5.1.78 |
Glutathionylspermidine amidase.
based on mapping to UniProt P0AES0
Glutathionylspermidine + H(2)O = glutathione + spermidine.
-!- Transforms glutathionylspermidine into glutathione and spermidine. -!- The enzyme from Escherichia coli is bifunctional and also catalyzes the reaction of EC 6.3.1.8, resulting in a net hydrolysis of ATP.
|
| 6.3.1.8 |
Glutathionylspermidine synthase.
based on mapping to UniProt P0AES0
Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate.
-!- Involved in the synthesis of trypanothione in trypanosomatids. -!- The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 3.5.1.78 reaction, resulting in a net hydrolysis of ATP.
|
UniProtKB Entries (1)
| P0AES0 |
GSP_ECOLI
Escherichia coli K-12
Bifunctional glutathionylspermidine synthetase/amidase
|
PDB Structure
| PDB | 3O98 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases
Protein Sci.
|