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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 ${\displaystyle \rightleftharpoons }$ 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) . 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

• 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.

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• EC 6.3.1
• Magnesium enzymes
• Enzymes of known structure
• Ligase stubs