Glutathionylspermidine synthase

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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 $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 6.3.1.8
BRENDA references for 6.3.1.8 (Recommended.)
PubMed references for 6.3.1.8
PubMed Central references for 6.3.1.8
Google Scholar references for 6.3.1.8
Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH (1992). "Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata". Protein. Sci. 1: 874–83. PMID 1304372.
Bollinger JM Jr, 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: 14031–41. PMID 7775463.