7432-24-8

Usage

Uses

Used in Pharmaceutical Industry:
H-GAMMA-GLU-PHE-OH is used as an active pharmaceutical ingredient for its potential therapeutic effects. It can be utilized in the development of drugs targeting specific diseases due to its ability to interact with various biological receptors and enzymes.
Used in Cosmetic Industry:
In the cosmetic industry, H-GAMMA-GLU-PHE-OH is used as a key ingredient in skincare and beauty products for its potential benefits in promoting skin health and appearance. It may be included in formulations to enhance skin hydration, improve skin texture, and provide antioxidant protection.
Used in Research and Development:
H-GAMMA-GLU-PHE-OH is used as a research tool in the field of biochemistry and molecular biology. It can be employed in laboratory experiments to study the interactions between peptides and their target molecules, as well as to investigate the mechanisms of various biological processes.
Used in Food Industry:
In the food industry, H-GAMMA-GLU-PHE-OH may be used as an additive or ingredient in the development of functional foods and beverages. It could potentially enhance the nutritional value, taste, or shelf life of these products, contributing to their overall quality and appeal.
Used in Agricultural Industry:
H-GAMMA-GLU-PHE-OH can be utilized in the agricultural industry as a component in the development of biopesticides or biofertilizers. Its incorporation into these products may help improve crop yield, enhance plant growth, or provide protection against pests and diseases.

InChI:InChI=1/C14H18N2O5/c15-10(13(18)19)6-7-12(17)16-11(14(20)21)8-9-4-2-1-3-5-9/h1-5,10-11H,6-8,15H2,(H,16,17)(H,18,19)(H,20,21)/t10-,11-/m0/s1

Upstream product

• 56-85-9 L-glutamine 
• 63-91-2 L-phenylalanine 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 86938-17-2 2-(S)-tert-butoxycarbonylaminopentanedioic acid 1-ethyl ester 

Downstream Products

• 56-86-0 L-glutamic acid 
• 63-91-2 L-phenylalanine 

Relevant academic research and scientific papers

Synthesis and sensory characteristics of kokumi ?-[Glu]n-Phe in the presence of glutamine and phenylalanine: Glutaminase from bacillus amyloliquefaciens or aspergillus oryzae as the catalyst

The transpeptidase activity of glutaminase from Bacillus amyloliquefaciens (GBA) and Aspergillus oryzae (GAO) to yield ?-[Glu]n-Phe peptides were verified for the first time. In the presence of Gln and Phe, ?-Glu-Phe and ?-Glu-?-Glu-Phe were synthesized by GAO, and ?-Glu-Phe, ?-Glu-?-Glu-Phe, ?-Glu-?-Glu-?-Glu-Phe, ?-Glu-?-Glu-?-Glu-?-Glu-Phe, and ?-Glu-?-Glu-?-Glu-?-Glu-?-Glu-Phe were synthesized by GBA. The Km values for the transpeptidation catalyzed by GBA and GAO were 47.88 and 153.92 mM (Phe as the acceptor), 84.89 and 236.47 mM (?-Glu-Phe as the acceptor), indicating that GBA had a greater affinity than GAO for Phe and ?-Glu-Phe in the transpeptidation reaction. The Km values for the transpeptidation catalyzed by GBA against acceptors, Phe and ?-[Glu](1≤na kokumi taste to commercial soy sauce and model chicken broth. The astringent threshold values (2.5-3.92 mM) were approximately 3-fold of the kokumi threshold concentrations (0.78-1.53 mM). ?-[Glu]n-Phe or the post-enzymatic reaction mixture enhanced the umami intensity of commercial soy sauce and model chicken broth.

γ-Glutamyl-dipeptides: Easy tools to rapidly probe the stereoelectronic properties of the ionotropic glutamate receptor binding pocket

γ-Glutamyl-dipeptides, built by condensing the distal carboxylate of L-Glu (or D-Glu) onto a series of differently functionalized amino acids, were prepared and used as tools for rapidly probing the stereo-electronic properties of iGluRs, searching for subtype-selective ligands.

PH-Dependent hydrolase, glutaminase, transpeptidase and autotranspeptidase activities of Bacillus subtilis γ-glutamyltransferase

γ-Glutamyltransferases (γ-GTs) are heterodimeric enzymes that catalyze the transfer of a γ-glutamyl group from a donor species to an acceptor molecule in a transpeptidation reaction through the formation of an intermediate γ-glutamyl enzyme. In our search for a γ-GT from a generally recognized as safe microorganism suitable for the production of γ-glutamyl derivatives with flavor-enhancing properties intended for human use, we cloned and overexpressed the γ-GT from Bacillus subtilis. In this study, we report the behavior of B. subtilis γ-GT in reactions involving glutamine as the donor compound and various acceptor amino acids. The common thread emerging from our results is a strong dependence of the hydrolase, transpeptidase and autotranspeptidase activities of B. subtilis γ-GT on pH, also in relation to the pKa of the acceptor amino acids. Glutamine, commonly referred to as a poor acceptor molecule, undergoes rapid autotranspeptidation at elevated pH, affording oligomeric species, in which up to four γ-glutamyl moieties are linked to a single glutamine. Moreover, we found that d-glutamine is also recognized both as a donor and as an acceptor substrate. Our results prove that the B. subtilis γ-GT-catalyzed transpeptidation reaction is feasible, and the observed activities of γ-GT from B. subtilis could be interpreted in relation to the known ability of the enzyme to process the polymeric material γ-polyglutamic acid.