2440-62-2

Basic information

• Product Name: N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE
• Synonyms: SUCCINYL-L-PHENYLALANINE 4-NITROANILIDE;SUC-PHENYLALANINE-PNA;SUC-PHE-PNA;N-SUCCINYL-L-PHENYALANINE-P-NITROANILIDE;N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE;Na-(3-Carboxypropionyl)-1-phenylalanine-4-nitroanilide;L-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE;N-succinyl-L-phenylalanine-P-*nitroanilide crysta
• CAS NO: 2440-62-2
• Molecular Formula: C₁₉H₁₉N₃O₆
• Molecular Weight: 385.37
• EINECS: 219-472-6
• Product Categories: Chymotrypsin, alpha;Chymotrypsin, alphaEnzyme Substrates;Enzyme Substrates;Protease Substrates;Substrates by Enzyme
• Mol File: 2440-62-2.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 769.3°C at 760 mmHg
• Flash Point: 419.1°C
• Appearance: /
• Density: 1.383g/cm³
• Vapor Pressure: 6.81E-25mmHg at 25°C
• Refractive Index: 1.636
• Storage Temp.: −20°C
• PKA: 4.68±0.10(Predicted)
• CAS DataBase Reference: N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE(CAS DataBase Reference)
• NIST Chemistry Reference: N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE(2440-62-2)
• EPA Substance Registry System: N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE(2440-62-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 2440-62-2(Hazardous Substances Data)

Usage

Uses

N-Succinyl-L-phenylalanine-p-nitroanilide has been used as a substrate for the hydrolytic activity of chymotrypsin and molar absorptive experiments. It has also been used for monitoring in vitro α-chymotrypsin inhibition assay.

Biochem/physiol Actions

N-Succinyl-L-phenylalanine-p-nitroanilide, a substrate for the hydrolytic activity of chymotrypsin, forms a yellow chromophore, p-nitroaniline, which can be measured spectrophotometrically at 410 nm.

InChI:InChI=1/C19H19N3O6/c23-17(10-11-18(24)25)21-16(12-13-4-2-1-3-5-13)19(26)20-14-6-8-15(9-7-14)22(27)28/h1-9,16H,10-12H2,(H,20,26)(H,21,23)(H,24,25)

Upstream product

• 108-30-5 succinic acid anhydride 
• 78106-64-6 H-Phe-pNA*HBr 
• 97885-48-8 N-(1,1-dimethylethoxycarbonyl)-L-phenylalanine N-(4-nitrophenyl)amide 
• 100-01-6 4-nitro-aniline 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 14235-15-5 benzyl (S)-(1-((4-nitrophenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 2360-97-6 L-phenylalanine-p-nitroanilide 

Downstream Products

• 863891-21-8 {2-[2-(2-{3-[(S)-1-(4-Nitro-phenylcarbamoyl)-2-phenyl-ethylcarbamoyl]-propionylamino}-ethoxy)-ethoxy]-ethoxy}-acetic acid 
• 796089-76-4 N-{2-[2-(2-amino-ethoxy)-ethoxy]-ethyl}-N'-[1-(4-nitro-phenylcarbamoyl)-2-phenyl-ethyl]-succinamide 
• 100-01-6 4-nitro-aniline 
• 37590-83-3 (S)-4-((1-carboxy-2-phenylethyl)amino)-4-oxobutanoic acid 

Relevant articles and documents

A molecular probe with both chromogenic and fluorescent units for detecting serine proteases

A molecular probe with L-phenylalanine p-nitroanilide and L-lysin 4-methylcoumaryl-7-amide, in which these amino acid derivatives are connected through a succinic-acid spacer, was prepared. Trypsin and papain were detected by blue-fluorescence emission of generated 7-amino-4-methylcoumarin (AMC). α-Chymotrypsin and nattokinase were detected from both the blue-fluorescence emission of AMC and the UV absorbance of p-nitroaniline. In addition, different time courses of p-nitroaniline and AMC were observed between the reaction of P1 with α-chymotrypsin and that with nattokinase. In the case of nattokinase, both the fluorescence emission and UV absorbance slowly increased. In contrast, the increasing UV absorbance was saturated at the early stage of the reaction of the present probe with chymotrypsin, whereas the fluorescence emission continuously increased in the following stages.

Kinetic study on conformational effect in hydrolysis of p-nitroanilides catalyzed by α-chymotrypsin

Effects of medium viscosity on kinetics for the hydrolysis of p-nitroanilides of certain amino acid derivatives catalyzed by α-chymotrypsin have been investigated. Observed data indicate that the overall rate constant, kcat, is hardly affected by the medium viscosity in all the substrates employed and equals the rate constant at the acylation step, k2, in the measured range of viscosity. By comparison with the data on p-nitrophenyl ester substrates reported previously, it is concluded that the formation of the tetrahedral intermediate in the course of the acylation of the enzyme is influenced by conformational change of the enzyme, whereas the breakdown of the intermediate is almost free from conformational effects.