Glutathionylspermidine synthase
glutathionylspermidine synthase | |||||||||
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Identifiers | |||||||||
EC number | 6.3.1.8 | ||||||||
CAS number | Template:CAS | ||||||||
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 / EGO | ||||||||
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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.
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
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