Z-D-norleucine 4-nitrophenyl ester
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Z-D-norleucine 4-nitrophenyl ester

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Category
CBZ-Amino Acids
Catalog number
BAT-005762
CAS number
31062-20-1
Molecular Formula
C20H22N2O6
Molecular Weight
386.40
Z-D-norleucine 4-nitrophenyl ester
IUPAC Name
(4-nitrophenyl) (2R)-2-(phenylmethoxycarbonylamino)hexanoate
Synonyms
Z-D-Nle-ONp; Z-D-2-aminohexanoic acid 4-nitrophenyl ester
Appearance
White to off-white solid
Purity
99%
Melting Point
69-72 °C
Storage
Store at 2-8°C
InChI
InChI=1S/C20H22N2O6/c1-2-3-9-18(21-20(24)27-14-15-7-5-4-6-8-15)19(23)28-17-12-10-16(11-13-17)22(25)26/h4-8,10-13,18H,2-3,9,14H2,1H3,(H,21,24)/t18-/m1/s1
InChI Key
UFQPOFZGPUCSGU-GOSISDBHSA-N
Canonical SMILES
CCCCC(C(=O)OC1=CC=C(C=C1)[N+](=O)[O-])NC(=O)OCC2=CC=CC=C2
1. 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.
3. 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.
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