Glutathionylspermidine amidase () is an enzyme characterised from Escherichia coli that catalyzes the hydrolysis of glutathionylspermidine to glutathione and spermidine:
The enzyme is bifunctional and in the reverse direction is equivalent to glutathionylspermidine synthase but requires adenosine triphosphate in that case.
This enzyme is a hydrolase, one 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).
Structural studies As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
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