50409-83-1

Basic information

• Product Name: S-mandelylglutathione
• Synonyms: S-mandelylglutathione;N-[N-(L-γ-Glutamyl)-S-mandeloyl-L-cysteinyl]glycine
• CAS NO: 50409-83-1
• Molecular Formula: C₁₈H₂₃N₃O₈S
• Molecular Weight: 441.46
• Mol File: 50409-83-1.mol

Chemical Properties

• Boiling Point: 859.9°C at 760 mmHg
• Flash Point: 473.8°C
• Appearance: /
• Density: 1.46g/cm³
• Vapor Pressure: 1.63E-31mmHg at 25°C
• Refractive Index: 1.615
• CAS DataBase Reference: S-mandelylglutathione(CAS DataBase Reference)
• NIST Chemistry Reference: S-mandelylglutathione(50409-83-1)
• EPA Substance Registry System: S-mandelylglutathione(50409-83-1)

Safety Data

• Hazardous Substances Data: 50409-83-1(Hazardous Substances Data)

Usage

InChI:InChI=1/C18H23N3O8S/c19-11(17(27)28)6-7-13(22)21-12(16(26)20-8-14(23)24)9-30-18(29)15(25)10-4-2-1-3-5-10/h1-5,11-12,15,25H,6-9,19H2,(H,20,26)(H,21,22)(H,23,24)(H,27,28)/t11-,12-,15?/m0/s1

Upstream product

• 67972-70-7 (S)-2-Amino-4-[(R)-1-(carboxymethyl-carbamoyl)-2-(1-hydroxy-2-oxo-2-phenyl-ethylsulfanyl)-ethylcarbamoyl]-butyric acid 
• 70-18-8 GLUTATHIONE 
• 1074-12-0 phenylglyoxal hydrate 

Downstream Products

• 90-64-2 d-(-)-mandelic acid 

Relevant articles and documents

S-2-Hydroxyacylglutathione-Derivatives: Enzymatic Preparation, Purification and Characterisation

S-2-Hydroxyacylglutathione derivatives have been prepared by enzymatic synthesis from α-oxoaldehydes and reduced glutathione in the presence of glyoxalase I.S-D-Lactoylglutathione, S-D-mandelylglutathione, S-glycolylglutathione and S-L-glyceroylglutathione were prepared from methylglyoxal, phenylglyoxal, glyoxal and hydroxypyruvaldehyde, respectively.They were purified by ion exchange chromatography on Dowex 1 on a gram scale.Analytical data and re-evaluated extinction coefficients for these compounds are presented.The method described provides a reliable, large-scale procedure for the preparation and purification of S-acylglutathiones of increasing biological and pharmacological interest.

Hammett Analysis of the Human Erythrocyte Glyoxalase I-Catalysed Rearrangement to Mandeloyl Thiolesters of Hemithioacetals formed from Glutathione and Substituted Arylglyoxals

Glyoxalase I (EC 4.4.1.5), purified to homogeneity from human erythrocytes, catalyses the rearrangement to α-hydroxymandeloylglutathiones of the hemithioacetals formed by equilibration of glutathione with para-substituted arylglyoxals.The association constants describing these equilibria were measured at 25 degC, pH 7.0.Values of kcat, Km and kcat/Km, describing the substrate behaviour of these hemithioacetals towards human erythrocyte glyoxalase I, were determined at pH 7.0 and 25 degC.Hammett analysis showed a linear correlation only for kcat(ρ+0.43)versus Hammett ? constants.Literature data for glyoxalase I from yeast showed similar behaviour (ρ+0.47).In both cases good correlation required exclusion of the unsubstituted phenylglyoxal data and consideration only of para-substituted substrates.A linear free energy relationship was found between kcat values for the human erythrocyte glyoxalase I-catasysed reaction and the rearrangement step for the model, non-enzymatic reaction.Comparisons of model and enzymatic cases on the basis of Hammett sensitivities and primary deuterium isotope effects indicated that both model and enzymatic transition states are probably closely similar and involve rate-determining deprotonation of the C-H bond adjacent to the sulphur atom in the hemithioacetal.

Reactions of Thiols with Phenylglyoxal to Give Thiomandelic S-Esters Formation of Hemithioacetals and Their Rearrangement

Equilibrium constants Kh for the addition of 2-mercaptoethanol and glutathione to phenylglyoxal to form hemithioacetals were determined spectrophotometrically over the pH range 7-10.The observed Kh values decrease sigmoidally with pH as the thiol ionizes.Rearrangement of hemithioacetals formed from phenylglyoxal and various thiols was kinetically investigated.The rates increase with thiol concentration following a saturation curve to give Kh identical with the spectrophotometric value.The rearrangement is subject to general base catalysis.The solvent isotope effect on the rate of the rearrangement, kH2O/kd2O, is nearly 1.0; that on the equilibrium, KH2Oh/KD2Oh, is 0.38.The results strongly support the mechanism involving proton transfers through an enediol intermediate.