N-α-Carbobenzoxy-L-glutamine 4-nitrophenyl ester
Need Assistance?
  • US & Canada:
    +
  • UK: +

N-α-Carbobenzoxy-L-glutamine 4-nitrophenyl ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category
CBZ-Amino Acids
Catalog number
BAT-005991
CAS number
7763-16-8
Molecular Formula
C19H19N3O7
Molecular Weight
401.37
N-α-Carbobenzoxy-L-glutamine 4-nitrophenyl ester
IUPAC Name
(4-nitrophenyl) (2S)-5-amino-5-oxo-2-(phenylmethoxycarbonylamino)pentanoate
Synonyms
Z-Gln-ONp
Purity
99%
Density
1.4±0.1 g/cm3
Boiling Point
690.4±55.0 °C
Storage
Store at -20 °C
InChI
InChI=1S/C19H19N3O7/c20-17(23)11-10-16(21-19(25)28-12-13-4-2-1-3-5-13)18(24)29-15-8-6-14(7-9-15)22(26)27/h1-9,16H,10-12H2,(H2,20,23)(H,21,25)/t16-/m0/s1
InChI Key
KIVQPDPRDVIJDJ-INIZCTEOSA-N
Canonical SMILES
C1=CC=C(C=C1)COC(=O)NC(CCC(=O)N)C(=O)OC2=CC=C(C=C2)[N+](=O)[O-]

N-α-Carbobenzoxy-L-glutamine 4-nitrophenyl ester, a versatile chemical compound with diverse applications in biochemistry and pharmaceutical research, assumes multifaceted roles across various domains.

Enzyme Assays: Functioning as a chromogenic substrate in enzyme assays, N-α-Carbobenzoxy-L-glutamine 4-nitrophenyl ester proves invaluable for investigating proteases like glutamyl endopeptidases. The enzymatic cleavage of this compound results in the release of 4-nitrophenol, triggering a visible color transformation that facilitates precise quantification of enzyme activity.

Protein Sequencing: Integral to the Edman degradation method for protein sequencing, this compound plays a pivotal role in the identification of N-terminal amino acids within peptides. By interacting with the terminal amino acid, it enables subsequent removal and identification, enabling step-by-step sequencing essential for unraveling the complex structure and function of proteins with surgical precision and unwavering accuracy.

Synthesis of Peptide Derivatives: Positioned at the forefront of organic chemistry, N-α-Carbobenzoxy-L-glutamine 4-nitrophenyl ester emerges as a key protagonist in peptide synthesis as a safeguarded glutamine derivative. Its utilization serves as a shield against undesirable reactions at the reactive sites of glutamine during peptide chain assembly, streamlining the production of precise peptide sequences for both research endeavors and therapeutic applications with enhanced precision and unwavering reliability.

Bioconjugation Studies: Carving a distinctive niche in the realm of bioconjugation, this compound assumes a pivotal role in crafting enzyme-linked probes and markers that enrich biocatalysis studies. Capable of conjugation with diverse molecules or proteins, it lays a robust foundation for exploring molecular interactions and biocatalytic mechanisms with extraordinary versatility. This versatility fuels the development of state-of-the-art diagnostic tools and empowers the exploration of biologically significant interactions within complex systems.

2. Human alpha-thrombin inhibition by the highly selective compounds N-ethoxycarbonyl-D-Phe-Pro-alpha-azaLys p-nitrophenyl ester and N-carbobenzoxy-Pro-alpha-azaLys p-nitrophenyl ester: a kinetic, thermodynamic and X-ray crystallographic study
G De Simone, G Balliano, P Milla, C Gallina, C Giordano, C Tarricone, M Rizzi, M Bolognesi, P Ascenzi J Mol Biol. 1997 Jun 20;269(4):558-69. doi: 10.1006/jmbi.1997.1037.
Kinetics, thermodynamics and structural aspects of human alpha-thrombin (thrombin) inhibition by newly synthesized low molecular weight derivatives of alpha-azalysine have been investigated. The thrombin catalyzed hydrolysis of N-ethoxycarbonyl-D-Phe-Pro-alpha-azaLys p-nitrophenyl ester (Eoc-D-Phe-Pro-azaLys-ONp) and N-carbobenzoxy-Pro-alpha-azaLys p-nitrophenyl ester (Cbz-Pro-azaLys-ONp) was investigated at pH 6.2 and 21.0 degrees C, and analyzed in parallel with that of N-alpha-(N,N-dimethylcarbamoyl)-alpha-azalysine p-nitrophenyl ester (Dmc-azaLys-ONp). Decarboxylation following the enzymatic hydrolysis of these p-nitrophenyl esters gave the corresponding 1-peptidyl-2(4-aminobutyl) hydrazines (peptidyl-Abh) showing properties of thrombin competitive inhibitors. Therefore, thermodynamics for the reversible binding of D-Phe-Pro-Abh, Cbz-Pro-Abh and Dmc-Abh to thrombin was examined. These results are consistent with the minimum four-step catalytic mechanism for product inhibition of serine proteinases. Eoc-D-Phe-Pro-azaLys-ONp and Eoc-D-Phe-Pro-Abh display a sub-micromolar affinity for thrombin together with a high selectivity versus homologous plasmatic and pancreatic serine proteinases acting on cationic substrates. The three-dimensional structures of the reversible non-covalent thrombin:Eoc-D-Phe-Pro-Abh and thrombin:Cbz-Pro-Abh complexes have been determined by X-ray crystallography at 2.0 A resolution (R-factor = 0.169 and 0.179, respectively), and analyzed in parallel with that of the thrombin:Dmc-azaLys acyl-enzyme adduct. Both Eoc-D-Phe-Pro-Abh and Cbz-Pro-Abh competitive inhibitors are accommodated in the thrombin active center, spanning the region between the aryl binding site and the S1 primary specificity subsite.
3. Thrombin inhibition by the highly selective 'reversible suicide substrate' N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester
Paolo Ascenzi, Carlo Gallina, Martino Bolognesi Protein Pept Lett. 2005 Jul;12(5):433-8. doi: 10.2174/0929866054395301.
Thrombin is the last enzyme in the blood coagulation cascade. All pharmacological aspects support the use of thrombin inhibitors as antithrombotic agents. Here, we review the unusual inhibition behavior of the highly selective 'reversible suicide substrate' N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester (Eoc-D-Phe-Pro-azaLys-ONp) targeted to the active center of human alpha-thrombin. Eoc-D-Phe-Pro-azaLys-ONp is an acylating agent, but its hydrolysis product 1(N-ethoxycarbonyl-D-phenylalanyl-L-prolyl)-2(4-aminobutyl) hydrazine behaves as a highly selective human alpha-thrombin competitive inhibitor.
Online Inquiry
Verification code
Inquiry Basket