2922-56-7

Usage

Uses

S-methylglutathione is a methionine containing peptide and glyoxylase inhibitor.

Biochem/physiol Actions

S-methylglutathione is a methionine containing peptide and glyoxylase inhibitor.

InChI:InChI=1/C11H19N3O6S/c1-21-5-7(10(18)13-4-9(16)17)14-8(15)3-2-6(12)11(19)20/h6-7H,2-5,12H2,1H3,(H,13,18)(H,14,15)(H,16,17)(H,19,20)/t6-,7-/m0/s1

Upstream product

• 74-87-3 methylene chloride 
• 70-18-8 GLUTATHIONE 
• 148-18-5 sodium N,N-diethyldithiocarbamate 
• 17356-08-0 thiourea 
• 74-88-4 methyl iodide 

Relevant academic research and scientific papers

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

A primary route of metabolism of dihalomethanes occurs via glutathione (GSH) transferase-catalyzed conjugation. Mammalian theta class GSH transferases and a group of bacterial dichloromethane dehalogenases are able to catalyze the hydrolytic dehalogenation of dihalomethanes via GSH conjugation and subsequent formation of HCHO. Dihalomethanes have been shown to induce revertants in Salmonella typhimurium TA 1535 expressing theta class GSH transferases. Two mammalian theta class GSH transferases (rat GST 5-5 and human GST T1) and the bacterial dehalogenase DM11 were compared in the in vitro conjugation of CH3Cl and using in vitro assays (HCHO formation) and the S. typhimurium mutagenesis assay with the dihalomethanes CH2Cl2, CH2Br2, CH2BrCl, CH2ICl, CH2I2, and CH2ClF. GSTs 5-5 and T1 had similar characteristics and exhibited first-order rather than Michaelis - Menten kinetics for HCHO formation over the range of dihalomethane concentrations tested. In contrast, the DM11 enzyme displayed typical hyperbolic Michaelis - Menten kinetics for all of the compounds tested. A similar pattern was observed for the conjugation of CH3Cl. The reversion tests with S. typhimurium expressing DM11 or GST 5-5 showed a concentration-dependent increase in revertants for most of the dihalomethanes, and DM11 produced revertants at dihalomethane concentrations lower than GST 5-5. Collectively, the results indicate that rates of conversion of dihalomethanes to HCHO are not correlated with mutagenicity and that GSH conjugates are genotoxic. The results are compared with the conjugation and genotoxicity of haloethanes in the preceding paper in this issue [Wheeler, J. B., Stourman, N. V., Armstrong, R. N., and Guengerich, F. P. (2001) Chem. Res. Toxicol. 14, 1107-1117]. The halide order appears most important in the dihalomethane conjugation reactions catalyzed by GST 5-5 and less so in GST T1 and DM11, probably due to changes in the rate-limiting steps.

Partial Methanolysis and Fast Atom Bombardment Mass Spectrometry of Peptides Containing Sulphurated Amino Acids

Sequence determination by partial methanolysis and fast atom bombardment (FAB) mass spectrometry of peptides containing cysteine and methionine was investigated.Cysteine-containing peptides require methylation of the sulphydryl group by methyl iodide to give a stable S-methylcysteinyl residue prior to partial methanolysis and mass spectrometry.Methionine-containing peptides undergo partially a methylation on sulphur during methanolysis, with formation of an S-methylsulphonium ion which under FAB conditions is extracted from the matrix and eliminates methyl sulphide in the gas phase.The presence of additional peaks due to chemical modifications or gas-phase fragmentations, however, does not interfere with sequence information of the spectra.

Kokumi-imparting agent

The present invention encompasses a method for screening for a kokumi-imparting substance by using the calcium receptor activity as an index, a composition containing a kokumi-imparting substance obtained by the screening method, a method for producing fo

PROPHYLACTIC OR THERAPEUTIC AGENT FOR DIARRHEA

A compound having calcium-receptor activation action can be used as an active ingredient of a prophylactic or therapeutic agent for diarrhea. The compound including a peptide such as γ-Glu-X-Gly (X represents an amino acid or an amino acid derivative), γ-

LOW-FAT FOOD

A low-fat food containing an amino acid or a peptide which is able to activate a calcium receptor, examples of which include γ-Glu-X-Gly, γ-Glu-Val-Y, γ-Glu-Ala, γ-Glu-Gly, γ-Glu-Cys, γ-Glu-Met, γ-Glu-Thr, γ-Glu-Val, γ-Glu-Orn, Asp-Gly, Cys-Gly, Cys-Met,

CALCIUM RECEPTOR ACTIVATOR

A calcium receptor activator containing one or more kinds of substances selected from á-Glu-Cys-Gly, á-Glu-Cys(SNO)-Gly, á-Glu-Ala, á-Glu-Gly, á-Glu-Cys, á-Glu-Met, á-Glu-Thr, á-Glu-Val, á-Glu-Orn, Asp-Gly, Cys-Gly, Cys-Met, Glu-Cys, Gly-Cys, Leu-Asp, D-Cys, á-Glu-Met(O), á-Glu-Val-Val, á-Glu-Val-Glu, á-Glu-Val-Lys, á-Glu- á-Glu-Val, á-Glu-Val-NH2, á-Glu-Val-ol, á-Glu-Ser, á-Glu-Tau, á-Glu-Cys(S-Me)(O), á-Glu-Leu, á-Glu-Ile, á-Glu-t-Leu, á-Glu-Cys(S-allyl)-Gly, á-Glu-Gly-Gly, á-Glu-Val-Phe, á-Glu-Val-Ser, á-Glu-Val-Pro, á-Glu-Val-Arg, á-Glu-Val-Asp, á-Glu-Val-Met, á-Glu-Val-Thr, á-Glu-Val-His, á-Glu-Val-Asn,á-Glu-Val-Gln, á-Glu-Val-Cys, á-Glu-Val-Orn, á-Glu-Ser-Gly, á-Glu-Cys(S-Me), á-Glu-Abu-Gly, á-Glu-Cys(S-Me)-Gly, and á-Glu-Val-Gly.

Reversibility of binding of cisplatin-methionine in proteins by diethyldithiocarbamate or thiourea: A study with model adducts

Model adducts for platinum-protein binding, i.e. at cysteine and methionine sites, have been synthesized by starting from [PtCl(dien)]Cl, cis-Pt(NH3)2Cl2, trans-Pt(NH3)2Cl2, and [PtCl(NH3)3]Cl. Glutathione (GSH) and 5-methylglutathione (GS-Me) were used to mimic the sulfur atoms in the proteins. At pH 11 both trans-Pt(NH3)2Cl2 and [PtCl(NH3)3]Cl form trans-Pti-(NH3)2(GS)2 upon reaction with 2 equiv of GS-. Only the intermediate [Pt(NH3)3GS]Cl was found to be relatively stable. The Pt-cysteine type bonds in [Pt(dien)GS]+ and in trans-Pt(NH3)2(GS)2 could not be reversed by sodium diethyldithiocarbamate (Na(ddtc)) and thiourea. On the other hand the Pt-methionine models [Pt(dien)GS-Me]2+ and cis-Pt(GS-Me) react fast with Na(ddtc) (f1/2 = 1/2 = 30 min-2 h), thereby restoring the original structure of the thioether linkage. The complex formed between Na(ddtc) and the liberated Pt(dien)2+ unit proved to be a complex in which the Pt-dien chelate ring is partially opened, leaving one NH2 noncoordinated. The ability of the nephrotoxicity inhibitors Na(ddtc) and thiourea to reverse Pt-protein adducts - these adducts are supposed to be the origin of nephrotoxicity of platinum antitumor compounds - is interpreted in terms of removing the platinum from methionine sulfurs only.