2440-62-2 Usage
Description
N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE, often abbreviated as N-SUCCINYL-L-PHE P-NITROANILIDE, is a synthetic compound commonly utilized in biochemical research and pharmaceutical development. It is a derivative of phenylalanine, an essential amino acid, with a succinyl group and a p-nitroaniline group attached. N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE is particularly known for its role in enzyme activity assays and serves as a valuable tool for studying the function and inhibition of specific enzymes.
Uses
Used in Enzyme Activity Assays:
N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE is used as a substrate for the hydrolytic activity of chymotrypsin, a serine protease enzyme. The compound is specifically designed to be cleaved by chymotrypsin, allowing researchers to measure the enzyme's activity and efficiency in catalyzing the hydrolysis reaction. This application is crucial for understanding the enzyme's role in various biological processes and its potential as a therapeutic target.
Used in Molar Absorptive Experiments:
In addition to its role in enzyme activity assays, N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE is also used in molar absorptive experiments. These experiments involve measuring the absorbance of light by a compound at specific wavelengths, which can provide valuable information about the compound's molecular structure and properties. The p-nitroaniline group in the compound absorbs light in the visible spectrum, making it an ideal candidate for such studies.
Used in In Vitro α-Chymotrypsin Inhibition Assays:
N-SUCCINYL-L-PHENYLALANINE P-NITROANILIDE is employed for monitoring in vitro α-chymotrypsin inhibition assays. These assays are essential for identifying and characterizing potential inhibitors of α-chymotrypsin, which can be useful in the development of new drugs targeting this enzyme. By measuring the decrease in hydrolytic activity of α-chymotrypsin in the presence of potential inhibitors, researchers can evaluate the effectiveness of these compounds in blocking the enzyme's function.
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.
Check Digit Verification of cas no
The CAS Registry Mumber 2440-62-2 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,4,4 and 0 respectively; the second part has 2 digits, 6 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 2440-62:
(6*2)+(5*4)+(4*4)+(3*0)+(2*6)+(1*2)=62
62 % 10 = 2
So 2440-62-2 is a valid CAS Registry Number.
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)
2440-62-2Relevant articles and documents
A molecular probe with both chromogenic and fluorescent units for detecting serine proteases
Ishida, Kirara,Nakamura, Yushi,Oe, Yohei,Ohta, Tetsuo
, (2021/06/18)
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
Kawai, Yasushi,Matsuo, Takashi,Ohno, Atsuyoshi
, p. 887 - 891 (2007/10/03)
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.
