Literature summary for 7.2.2.13 extracted from

Krinulovic, K.S.; Vasic, V.M.
Interaction of some Pd(II) complexes with Na+ /K+-ATPase: inhibition, kinetics, prevention and recovery (2006), J. Enzyme Inhib. Med. Chem., 21, 459-465.

Search for more literature for 7.2.2.13

Inhibitors

Inhibitors	Comment	Organism	Structure
[PdCl(dien)]+	noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition	Sus scrofa
[PdCl(Me4dien)]+	noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition	Sus scrofa
[PdCl4]2-	noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	commercial product	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
cerebral cortex	-	Sus scrofa	-

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0121	-	pH 7.4, 37°C	Sus scrofa	[PdCl(dien)]+
0.0225	-	pH 7.4, 37°C	Sus scrofa	[PdCl4]2-
0.0236	-	pH 7.4, 37°C	Sus scrofa	[PdCl(Me4dien)]+

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)