Glycine, L-g-glutamyl-S-[(4-nitrophenyl)methyl]-L-cysteinyl-
![Glycine, L-g-glutamyl-S-[(4-nitrophenyl)methyl]-L-cysteinyl- Structure](https://image.chemsrc.com/caspic/117/6803-19-6.png)
Glycine, L-g-glutamyl-S-[(4-nitrophenyl)methyl]-L-cysteinyl- structure
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Common Name | Glycine, L-g-glutamyl-S-[(4-nitrophenyl)methyl]-L-cysteinyl- | ||
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| CAS Number | 6803-19-6 | Molecular Weight | 442.44400 | |
| Density | 1.464g/cm3 | Boiling Point | 877.1ºC at 760 mmHg | |
| Molecular Formula | C17H22N4O8S | Melting Point | N/A | |
| MSDS | N/A | Flash Point | 484.2ºC | |
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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 X-ray diffraction. In addition two complexes with glutathi... |
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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 analysis. The structure of the modified enzyme described here... |
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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 of all three thiols. We confirm that C47 is the 'fast' thio... |
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Intestinal glutathione transport system: a possible detoxication role.
Biochim. Biophys. Acta 1073(3) , 571-9, (1991) The epithelium of the small intestine act by the formation of GSH-S-conjugation, as a first line of defence against various ingested toxic chemicals. GSH and GSH-dependent enzymes are present in the gastrointestinal wall. We and others have characterized the ... |
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Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds.
Biochemistry 40(45) , 13564-73, (2001) The [URE3] phenotype in yeast Saccharomyces cerevisiae is due to an altered prion form of Ure2p, a protein involved in nitrogen catabolism. To understand possible conformational changes at the origin of prion propagation, we previously solved the crystal stru... |
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Sequential enzyme-catalyzed metabolism of 4-nitrotoluene to S-(4-nitrobenzyl)glutathione.
Biochem. Biophys. Res. Commun. 114(2) , 500-4, (1983) [14C]-4-Nitrotoluene was metabolized by rat liver postmitochondrial supernatant containing NADPH, reduced glutathione and a sulfate activating system to 4-nitrobenzyl alcohol, 4-nitrobenzyl sulfate, and S-(4-nitrobenzyl) glutathione. Formation of both sulfur-... |