13640-39-6

Basic information

• Product Name: H-GAMMA-GLU-GLY-GLY-OH
• Synonyms: H-GAMMA-GLU-GLY-GLY-OH;H-GLU(GLY-GLY)-OH;H-GLU(GLY-GLY-OH)-OH;L-GAMMA-GLUTAMYL-GLYCYL-GLYCINE;gamma-glutamyl-glycyl-glycine;L-Y-GLUTAMYL-GLYCYL-GLYCINE;Glu-Gly-gly;Glycine, N-(N-L-gamma-glutamylglycyl)-
• CAS NO: 13640-39-6
• Molecular Formula: C₉H₁₅N₃O₆
• Molecular Weight: 261.23
• Mol File: 13640-39-6.mol
• Article Data: 5

Chemical Properties

• Boiling Point: 749°Cat760mmHg
• Flash Point: 406.8°C
• Appearance: /
• Density: 1.433g/cm³
• Vapor Pressure: 1.5E-24mmHg at 25°C
• Refractive Index: 1.544
• Storage Temp.: -15°C
• CAS DataBase Reference: H-GAMMA-GLU-GLY-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-GAMMA-GLU-GLY-GLY-OH(13640-39-6)
• EPA Substance Registry System: H-GAMMA-GLU-GLY-GLY-OH(13640-39-6)

Safety Data

• Hazardous Substances Data: 13640-39-6(Hazardous Substances Data)

Usage

General Description

H-GAMMA-GLU-GLY-GLY-OH is a chemical compound consisting of four amino acids linked together in a specific sequence. It is a peptide with a linear structure, containing the amino acids gamma-glutamic acid (GAMMA), glycine (GLY), and a terminal hydroxyl group (OH). H-GAMMA-GLU-GLY-GLY-OH is often used in biochemical and pharmaceutical research as a model peptide for studying the structure-function relationships of proteins and peptides. It may also have potential applications in drug development or as a biochemical tool for understanding biological processes related to protein interaction and signaling pathways.

InChI:InChI=1/C9H15N3O6/c10-5(9(17)18)1-2-6(13)11-3-7(14)12-4-8(15)16/h5H,1-4,10H2,(H,11,13)(H,12,14)(H,15,16)(H,17,18)

Upstream product

• 56-85-9 L-glutamine 
• 556-50-3 glycylglycine 
• 70-18-8 GLUTATHIONE 
• 132433-10-4 L-γ-glutamyl-2,2,2-trifluoroethylamide 
• 916134-37-7 N^δ-(2-methoxy-2-oxoethyl)-L-glutamine 
• 916058-09-8 L-γ-glutamyl-2-(ethylthio)ethylamide trifluoroacetic acid salt 
• 87379-96-2 L-γ-glutamylglycinamide 
• 14235-10-0 N-(γ-L-glutamyl)propylamine 
• 7300-59-6 L-glutamic acid 5-(4-nitroanilide) 
• 10148-81-9 L-γ-glutamyl-L-glutamine 
• 58238-68-9 L-γ-glutamyl p-nitrophenyl ester 

Downstream Products

• 56-86-0 L-glutamic acid 
• 556-50-3 glycylglycine 

Relevant articles and documents

γ-Glutamyl Transfer Reactions by Glutaminase from Pseudomonas nitroreducens IFO 12694 and Their Application for the Syntheses of Theanine and γ-Glutamylmethylamide

In a mixture containing γ-glutamyl donor (donor) and γ-glutamyl acceptor (acceptor), the glutaminase of Pseudomonas nitroreducens IFO 12694 simultaneously catalyzed a γ-glutamyl transfer reaction and hydrolysis of the donor. The variation of the activities responding to the concentration of glutathione and glycylglycine indicated that the enzyme might be classified in a group of glutaminases that shows hydrolysis prior to transfer reaction. On the other hand, the results with glutamine and ethylamine or methylamine indicated that the enzyme was active in the transfer reaction with suppressed hydrolysis of glutamine, and suggested the possibility of using the reaction for producing γ-glutamylethylamide (theanine) or γ-glutamylmethylamide (γ-GMA). In fact, in a mixture containing high concentrations of substrates (0.7 M glutamine, 1.5 M ethylamine or methylamine) and 0.5 unit/ml glutaminase (borate buffer pH 11), 270 mM (47 g/L) theanine or 250 mM (38 g/L) γ-GMA was formed in 7 h of incubation at 30°C.

Molecular cloning and characterization of γ-Glutamyltranspeptidase from pseudomonas nitroreducens IFO12694

y-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694 (PnGGT) exhibited higher hydro-lytic activity than transfer activity, as compared with other y-glutamyltranspeptidases (GGTs). PnGGT showed little activity towards most of L-amino acids and towards glycyl-glycine, which is often used as a standard y-glutamyl accepter in GGT transfer reactions. The preferred substrates for PnGGT as a y-glutamyl accepter were amines such as methylamine, ethylamine, and isopropylamine.

Purification and properties of two isozymes of gamma-glutamyltranspeptidase from Bacillus subtilis TAM-4.

Two isozymes of gamma-glutamyltranspeptidase, GGT-A and GGT-B, were purified to electrophoretic homogeneity from a culture broth of Bacillus subtilis TAM-4, which produces poly(gamma-glutamic acid) (PGA) de novo. GGT-A was composed of three subunits with molecular weights of 23,000 (I), 39,000 (II), and 40,000 (III). GGT-B was composed of two subunits with molecular weight of 22,000 (I) and 39,000 (II). The N-terminal amino acid sequences of GGT-A subunit I and GGT-B subunit I were very similar. GGT-A subunit II and GGT-B subunit II had an identical N-terminal amino acid sequence. That of GGT-A subunit III showed no similarity to the other subunits. Both GGTs had similar enzymatic properties (optimum pH and temperature: pH 8.8 and 55 degrees C) but showed a significantly different thermal stability at 55 degrees C. Both GGT-A and -B used D-gamma-glutamyl-p-nitroanilide as well as the L-isomer as the gamma-glutamyl donor and used various amino acids and peptides as the acceptor. It was also found that the PGA produced by the strain was hydrolyzed to glutamic acid by its own GGTs.