Literature summary for 1.15.1.1 extracted from

Ye, M.; English, A.M.
Binding of polyaminocarboxylate chelators to the active-site copper inhibits the GSNO-reductase activity but not the superoxide dismutase activity of Cu,Zn-superoxide dismutase (2006), Biochemistry, 45, 12723-12732.

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Inhibitors

Inhibitors	Comment	Organism	Structure
DTPA	i.e. diethylenetriamine-N,N,N,N,N-pentaacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity	Bos taurus
EDTA	i.e. diethylenediamine-N,N,N,N-tetraacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	commercial prepapration, enzyme additionally catalyzes the reductive decomposition of S-nitroso-L-glutathione in presence of thiols	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
erythrocyte	-	Bos taurus	-

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Release 2023.1 (January 2023)