Biology:Glutathionylspermidine amidase
| glutathionylspermidine amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.78 | ||||||||
| CAS number | 171040-71-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glutathionylspermidine amidase (EC 3.5.1.78) is an enzyme that catalyzes the chemical reaction
- glutathionylspermidine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] glutathione + spermidine
Thus, the two substrates of this enzyme are glutathionylspermidine and H2O, whereas its two products are glutathione and spermidine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine amidase. This enzyme is also called glutathionylspermidine amidohydrolase (spermidine-forming). This enzyme participates in glutathione metabolism.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2IO7, 2IO8, 2IO9, 2IOA, and 2IOB.
References
- "Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase". J. Biol. Chem. 270 (23): 14031–41. 1995. doi:10.1074/jbc.270.23.14031. PMID 7775463.
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