Glycine, L-g-glutamyl-S-[(4-nitrophenyl)methyl]-L-cysteinyl-

Names

[ Name ]:
Glycine, L-g-glutamyl-S-[(4-nitrophenyl)methyl]-L-cysteinyl-

[Synonym ]:
s-(p-nitrobenzyl)glutathione

Biological Activity

[Description]:

S-(p-Nitrobenzyl)glutathione is a competitive glutathionase inhibitor. S-(p-Nitrobenzyl)glutathione is converted to the corresponding cysteine derivatives by rat kidney microsomes. S-(p-Nitrobenzyl)glutathione can be used for the research of metabolic breakdown of glutathione by the glutathionase system[1][2].

[Related Catalog]:

Signaling Pathways >> Others >> Others

Research Areas >> Metabolic Disease

Chemical & Physical Properties

[ Density]:
1.464g/cm3

[ Boiling Point ]:
877.1ºC at 760 mmHg

[ Molecular Formula ]:
C₁₇H₂₂N₄O₈S

[ Molecular Weight ]:
442.44400

[ Flash Point ]:
484.2ºC

[ Exact Mass ]:
442.11600

[ PSA ]:
229.94000

[ LogP ]:
1.71100

[ Index of Refraction ]:
1.618

MSDS

Click to get detail MSDS

Safety Information

Articles

Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors.

J. Mol. Biol. 237(3) , 298-314, (1994)

The three-dimensional crystal structure of pi class glutathione S-transferase YfYf from mouse liver complexed with the inhibitor S-(p-nitrobenzyl)glutathione has been determined at 1.8 A resolution by...

The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region.

J. Biol. Chem. 273(5) , 2844-50, (1998)

The three-dimensional structure of mouse liver glutathione S-transferase P1-1 carboxymethylated at Cys-47 and its complex with S-(p-nitrobenzyl)glutathione have been determined by x-ray diffraction an...

Site-directed mutagenesis of mouse glutathione transferase P1-1 unlocks masked cooperativity, introduces a novel mechanism for 'ping pong' kinetic behaviour, and provides further structural evidence for participation of a water molecule in proton abstraction from glutathione.

FEBS J. 278(2) , 273-81, (2011)

Mouse liver glutathione transferase P1-1 has three cysteine residues at positions 14, 47 and 169. We have constructed the single, double and triple cysteine to alanine mutants to define the behaviour ...