1955-67-5

Usage

Uses

Used in Enzyme Activity Assays:
AMINO ACID HYDROXAMATES L-GLUTAMIC ACID GAMMA-MONOHYDROXAMATE is used as a standard to calculate transglutaminase (TGase) activity. This application is crucial in the field of biochemistry and molecular biology, as it helps researchers understand the function and regulation of TGase enzymes, which are involved in various cellular processes, including protein cross-linking and signal transduction.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, AMINO ACID HYDROXAMATES L-GLUTAMIC ACID GAMMA-MONOHYDROXAMATE may be used as a starting material or intermediate in the synthesis of various drugs and therapeutic agents. Its unique structure and properties make it a valuable component in the development of novel pharmaceutical compounds.
Used in Research and Development:
AMINO ACID HYDROXAMATES L-GLUTAMIC ACID GAMMA-MONOHYDROXAMATE is also used in research and development for studying the structure, function, and interactions of various proteins and enzymes. Its ability to act as a standard for TGase activity assays makes it an essential tool for researchers working on protein function and enzyme mechanisms.

Biochem/physiol Actions

L-Glutamic acid γ-monohydroxamate [L-Glu(gamma)HXM] is used as a vanadium ligand which potentiates vanadiums metabolic activity. L-Glu(gamma)HXM is also used as a substrate for E. coli asparagine synthetase B and as an ATP-dependent irreversible inhibitor of Escherichia coli gamma-glutamylcysteine synthetase.

InChI:InChI=1/C5H10N2O4/c6-4(8)2-1-3(7-11)5(9)10/h3,7,11H,1-2H2,(H2,6,8)(H,9,10)/t3-/m0/s1

Upstream product

• 3183-72-0 N-γ-L-glutamyl-4-aminobutyric acid 
• 56-85-9 L-glutamine 
• 70-18-8 GLUTATHIONE 
• 142-47-2 monosodium L-glutamate 
• 10148-81-9 L-γ-glutamyl-L-glutamine 
• 56-86-0 L-glutamic acid 
• 1119-33-1 (S)-2-Amino-pentanedioic acid 5-ethyl ester 

Downstream Products

• 56-86-0 L-glutamic acid 
• 20292-78-8 amino phosphoric acid 
• 98-79-3 L-Pyroglutamic acid 

Relevant academic research and scientific papers

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.

Characterization of theanine-forming enzyme from Methylovorus mays No. 9 in respect to utilization of theanine production

For development of theanine production from glutamic acid and ethylamine by coupling yeast sugar fermentation as an ATP-regenerating system, several strains were selected from among about 200 methylamine- and/or methanol-assimilating bacteria depending on the theanine-forming activity of their permeated cells. The amount of theanine formed by the cells of the selected strains was much larger than that by the cells of Escherichia coli AD494 (DE3) expressing Pseudomonas taetrolens Y-30 glutamine synthetase (GS), which has been found to be a usable enzyme for theanine production. A GS-like enzyme responsible for the theanine-forming reaction was obtained from an obligate methylotroph isolate, Methylovorus mays No. 9. The enzyme was induced by methylamine in the culture medium. A molecular mass of 410-470 kDa was obtained by gel filtration of the enzyme, and 51 kDa by SDS-PAGE analysis. The enzyme showed high activity toward methylamine rather than ammonia, which indicates that it is similar to known γ-glutamylmethylamide synthetase. The isolated enzyme also had high reactivity to ethylamine in a neutral pH range, and formed theanine from glutamic acid and ethylamine in a reaction mixture containing a yeast sugar fermentation system for ATP-regeneration.

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.

Drug Latentiation by γ-Glutamyl Transpeptidase

The N-γ-glutamyl derivatives of L-thiazolidine-4-carboxylic acid, 4-aminobutyric acid, 1-aminocyclopentanecarboxylic acid, 2-aminophenol, and p-fluoro-L-phenylalanine (compounds 6, 8, 9, 10, and 12 respectively) were synthesized using the synthom phthaloylglutamic anhydride.Their relative rates of cleavage by the enzyme γ-glutamyl transpeptidase (γ-GT) were determined in order to evaluate the possibility for their selective release by this enzyme which is elevated in certain pathological conditions.Compounds 6, 8, and 9 were not readily solvolyzed by γ-GT, but compounds 10 and 12, as well as the N-γ-glutamylated derivatives of 3- and 4-aminophenol, were readily cleaved.