67413-34-7

Basic information

• Product Name: Z-GLU(OBZL)-OSU
• Synonyms: Z-L-GLUTAMIC ACID GAMMA-BENZYL ESTER ALPHA-N-HYDROXYSUCCINIMIDE ESTER;Z-GLUTAMIC ACID(OBZL)-OSU;Z-GLU(OBZL)-OSU;Z-L-Glu(OBzl)-OSu;Z-L-glutamic acid γ-benzyl ester α-N-hydroxysuccinimide ester≥ 97% (TLC)
• CAS NO: 67413-34-7
• Molecular Formula: C₂₄H₂₄N₂O₈
• Molecular Weight: 468.46
• Mol File: 67413-34-7.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Density: 1.36±0.1 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 10.35±0.46(Predicted)
• CAS DataBase Reference: Z-GLU(OBZL)-OSU(CAS DataBase Reference)
• NIST Chemistry Reference: Z-GLU(OBZL)-OSU(67413-34-7)
• EPA Substance Registry System: Z-GLU(OBZL)-OSU(67413-34-7)

Safety Data

• Hazardous Substances Data: 67413-34-7(Hazardous Substances Data)

Usage

Chemical Properties

Colorless oil

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 5680-86-4 N-benzyloxycarbonyl-5-O-benzyl-L-glutamic acid 

Downstream Products

• 75898-60-1 benzyloxycarbonyl-γ-benzyl-α-L-glutamyl-D-glutamine 
• 159790-69-9 bis(γ-benzyl) (benzyloxycarbonyl-α-L-glutamyl)-L-glutamate 
• 503130-00-5 C₃₇H₅₀N₅O₂₀P₃ 

Relevant articles and documents

Synthesis of non-hydrolyzable substrate analogs for Asp-tRNAAsn/Glu-tRNAGln amidotransferase

Non-hydrolyzable substrate analogs for tRNA-dependent amidotransferase, 2′- or 3′-aspartyl or -glutamyl adenosine, were synthesized from adenosine without protection of the adenine base. The hydroxyl groups of adenosine were selectively protected, followed by a series of oxidation/reductions to alter the stereochemistry. DFT calculations revealed the driving forces for the ketone hydrate formation at C-2′, but not the C-3′ carbon during the oxidation step. Subsequently, triflation and azide replacement yielded azidoadenosines, which were coupled to protected amino acids after deprotection and reduction. After global deprotection, the target substrate analogs were obtained in 2-14% overall yields from adenosine.

Synthesis of γ-Glutamyl Peptides Catalyzed by Transamidase from Bacillus natto

Crude ammonium sulfate fraction of a cell free extract from Bacillus natto contained an enzyme (or enzymes) which catalyzed the transamidation reaction specific for glutamine.Both L- and D-isomers of glutamine were active as substrate.On incubation of L- or D-glutamine with the enzyme preparation, two peptides consisting of glutamic acid and glutamine were formed.The main component of the peptides was readily isolated by ion-exchange chromatography and identified as γ-glutamylglutamine by paper chromatography and by paper electrophoresis using authentic peptides.The optical configuration of the amino acid residues in the dipeptide was determined by digestion of the acid hydrolyzate with L-glutamic acid decarboxylase, and the result showed that the dipeptide obtained from L-glutamine was a L-L isomer, while the dipeptide from D-glutamine was a D-D isomer.