128129-59-9

Basic information

• Product Name: L-gamma-glutamyl-(5S)-N~6~-(carboxymethyl)-5-(L-gamma-glutamylamino)-6-oxo-2,5-bis(sulfanylmethyl)-L-lysylglycine
• CAS NO: 128129-59-9
• Molecular Formula: C₂₂H₃₆N₆O₁₂S₂
• Molecular Weight: 640.6842
• Mol File: 128129-59-9.mol

Chemical Properties

• Boiling Point: 1220.5°C at 760 mmHg
• Flash Point: 691.9°C
• Density: 1.489g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.601
• CAS DataBase Reference: L-gamma-glutamyl-(5S)-N~6~-(carboxymethyl)-5-(L-gamma-glutamylamino)-6-oxo-2,5-bis(sulfanylmethyl)-L-lysylglycine(CAS DataBase Reference)
• NIST Chemistry Reference: L-gamma-glutamyl-(5S)-N~6~-(carboxymethyl)-5-(L-gamma-glutamylamino)-6-oxo-2,5-bis(sulfanylmethyl)-L-lysylglycine(128129-59-9)
• EPA Substance Registry System: L-gamma-glutamyl-(5S)-N~6~-(carboxymethyl)-5-(L-gamma-glutamylamino)-6-oxo-2,5-bis(sulfanylmethyl)-L-lysylglycine(128129-59-9)

Safety Data

• Hazardous Substances Data: 128129-59-9(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
L-gamma-glutamyl-(5S)-N~6~-(carboxymethyl)-5-(L-gamma-glutamylamino)-6-oxo-2,5-bis(sulfanylmethyl)-L-lysylglycine is used as a pharmaceutical compound for its potential role in protein synthesis and enzyme function. Its complex structure and the presence of multiple amino acid residues and functional groups make it a promising candidate for the development of new drugs and therapies.
Used in Biochemistry Research:
In the field of biochemistry, L-gamma-glutamyl-(5S)-N~6~-(carboxymethyl)-5-(L-gamma-glutamylamino)-6-oxo-2,5-bis(sulfanylmethyl)-L-lysylglycine is utilized as a research tool to study the interactions between amino acids, peptides, and enzymes. Its unique structure allows scientists to investigate the role of sulfhydryl groups and other functional groups in various biological processes, contributing to a deeper understanding of peptide chemistry and its applications.

Upstream product

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• 107-04-0 1-Bromo-2-chloroethane 
• 107-06-2 1,2-dichloro-ethane 

Relevant articles and documents

Conjugation of haloalkanes by bacterial and mammalian glutathione transferases: Mono- and vicinal dihaloethanes

Glutathione (GSH) transferases are generally involved in the detoxication of xenobiotic chemicals. However, conjugation can also activate compounds and result in DNA modification. Activation of 1,2-dihaloethanes (BrCH2CH2Br, BrCH2CH2Cl, and ClCH2CH2Cl) was investigated using two mammalian theta class GSH transferases (rat GST 5-5 and human GST T1) and a bacterial dichloromethane dehalogenase (DM11). Although the literature suggests that the bacterial dehalogenase does not catalyze reactions with CH3Cl, ClCH2CH2Cl, or CH3CHCl2, we found a higher enzyme efficiency for DM11 than for the mammalian GSH transferases in conjugating CH3Cl, CH3CH2Cl, and CH3CH2Br. Enzymatic rates of activation of 1,2-dihaloethanes were determined in vitro by measuring S,S-ethylene-bis-GSH, the major product trapped by nonenzymatic reaction with the substrate GSH. Salmonella typhimurium TA 1535 systems expressing each of these GSH transferases were used to determine mutagenicity. Rates of formation of S,S-ethylene-bis-GSH by the GSH transferases correlated with the mutagenicity determined in the reversion assays for the three 1,2-dihaloethanes, consistent with the view that half-mustards are the mutagenic products of the GSH transferase reactions. Half-mustards [S-(2-haloethyl)GSH] containing either F, Cl, or Br (as the leaving group) were tested for their abilities to induce revertants in S. typhimurium, and rates of hydrolysis were also determined. GSH transferases do not appear to be involved in the breakdown of the half-mustard intermediates. A halide order (Br > Cl) was observed for both GSH transferase-catalyzed mutagenicity and S,S-ethylene-bis-GSH formation from 1,2-dihaloethanes, with the single exception (both assays) of BrCH2CH2Cl reaction with DM11, which was unexpectedly high. The lack of substrate saturation seen for conjugation of dihalomethanes with GSTs 5-5 and T1 was also observed with the mono- and 1,2-dihaloethanes [Wheeler, J. B., Stourman, N. V., Thier, R., Dommermuth, A., Vuilleumier, S., Rose, J. A., Armstrong, R. N., and Guengerich, F. P. (2001) Chem. Res. Toxicol. 14, 1118-1127], indicative of an inherent difference in the catalytic mechanisms of the bacterial and mammalian GSH transferases.