7432-24-8

Basic information

• Product Name: H-GAMMA-GLU-PHE-OH
• Synonyms: H-GLU(PHE)-OH;H-GLU(PHE-OH)-OH;H-GAMMA-GLU-PHE-OH;N-L-gamma-glutamyl-3-phenyl-L-alanine;(2S)-2-amino-5-[[(2S)-1-hydroxy-1-oxo-3-phenylpropan-2-yl]amino]-5-oxopentanoic acid;Glutamylphenylalanine;gamma-glutamylphenylalanine;L-Y-GLUTAMYL-L-PHENYLALANINE
• CAS NO: 7432-24-8
• Molecular Formula: C₁₄H₁₈N₂O₅
• Molecular Weight: 294.3
• EINECS: 231-077-0
• Mol File: 7432-24-8.mol
• Article Data: 4

Chemical Properties

• Melting Point: 194-197 °C
• Boiling Point: 622 °C at 760 mmHg
• Flash Point: 330 °C
• Appearance: /
• Density: 1.332 g/cm³
• Vapor Pressure: 2.47E-16mmHg at 25°C
• Refractive Index: 1.582
• Storage Temp.: -15°C
• PKA: 2.22±0.10(Predicted)
• CAS DataBase Reference: H-GAMMA-GLU-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-GAMMA-GLU-PHE-OH(7432-24-8)
• EPA Substance Registry System: H-GAMMA-GLU-PHE-OH(7432-24-8)

Safety Data

• Hazardous Substances Data: 7432-24-8(Hazardous Substances Data)

Usage

Definition

ChEBI: A dipeptide obtained by formal condensation of the side-chain carboxy group of L-glutamic acid with the amino group of L-phenylalanine.

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 articles and documents

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.

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.