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 | 3A30 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Protein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetASE/amidase in redox regulation
J.Biol.Chem.
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