| Glutathionylspermidine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.8 | ||||||||
| CAS no. | 9077-09-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glutathionylspermidine synthase ( EC 6.3.1.8) is an enzyme that catalyzes the chemical reaction
- glutathione + spermidine + ATP glutathionylspermidine + ADP + phosphate
The 3 substrates of this enzyme are glutathione, spermidine, and ATP, whereas its 3 products are glutathionylspermidine, ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]. This enzyme is also called glutathione:spermidine ligase (ADP-forming). This enzyme participates in glutathione metabolism. It employs one cofactor, magnesium.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2IO7, 2IO8, 2IO9, 2IOA, and 2IOB.
- Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH (1992). "Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata". Protein Sci. 1 (7): 874–83. doi: 10.1002/pro.5560010705. PMC 2142158. PMID 1304372.
- Bollinger JM, Kwon DS, Huisman GW, Kolter R, Walsh CT (1995). "Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase". J. Biol. Chem. 270 (23): 14031–41. doi: 10.1074/jbc.270.23.14031. PMID 7775463.
| Glutathionylspermidine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.8 | ||||||||
| CAS no. | 9077-09-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glutathionylspermidine synthase ( EC 6.3.1.8) is an enzyme that catalyzes the chemical reaction
- glutathione + spermidine + ATP glutathionylspermidine + ADP + phosphate
The 3 substrates of this enzyme are glutathione, spermidine, and ATP, whereas its 3 products are glutathionylspermidine, ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]. This enzyme is also called glutathione:spermidine ligase (ADP-forming). This enzyme participates in glutathione metabolism. It employs one cofactor, magnesium.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2IO7, 2IO8, 2IO9, 2IOA, and 2IOB.
- Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH (1992). "Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata". Protein Sci. 1 (7): 874–83. doi: 10.1002/pro.5560010705. PMC 2142158. PMID 1304372.
- Bollinger JM, Kwon DS, Huisman GW, Kolter R, Walsh CT (1995). "Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase". J. Biol. Chem. 270 (23): 14031–41. doi: 10.1074/jbc.270.23.14031. PMID 7775463.