830-03-5

Basic information

• Product Name: 4-NITROPHENYL ACETATE
• Synonyms: 4-Nitrophenylacetat;4-Nitropheyl acetate;Acetic acid, p-nitrophenyl ester;aceticacid,p-nitrophenylester;Essigsαure-4-nitrophenylester;Phenol, p-nitro-, acetate;Phenol,p-nitro-,acetate;p-Nitrobenzene acetate
• CAS NO: 830-03-5
• Molecular Formula: C₈H₇NO₄
• Molecular Weight: 181.15
• EINECS: 212-593-5
• Product Categories: NA - NI;Alphabetic;Analytical Standards;Analytical/Chromatography;Bioactive Small Molecules;Building Blocks;C8 to C9;Carbonyl Compounds;Cell Biology;Chemical Synthesis;Esters;N;Organic Building Blocks
• Mol File: 830-03-5.mol
• Article Data: 166

Chemical Properties

• Melting Point: 75-77 °C(lit.)
• Boiling Point: 314.24°C (rough estimate)
• Flash Point: 145.2°C
• Appearance: Green/Powder
• Density: 1.4283 (rough estimate)
• Vapor Pressure: 0.0014mmHg at 25°C
• Refractive Index: 1.5468 (estimate)
• Storage Temp.: −20°C
• Solubility: 0.53g/l
• Water Solubility: Insoluble in water.
• Stability: Stable. Combustible. Incompatible with strong oxidizing agents.
• BRN: 515874
• CAS DataBase Reference: 4-NITROPHENYL ACETATE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-NITROPHENYL ACETATE(830-03-5)
• EPA Substance Registry System: 4-NITROPHENYL ACETATE(830-03-5)

Safety Data

• Hazard Codes: F,C
• Statements: 11-34
• Safety Statements: 24/25-45-36/37/39-26-16
• WGK Germany: 3
• RTECS: AJ1150000
• TSCA: Yes
• Hazardous Substances Data: 830-03-5(Hazardous Substances Data)

Usage

Description

4-Nitrophenyl Acetate is an organic compound that serves as a versatile substrate for various enzymatic assays and chemical reactions. It is characterized by its ability to undergo hydrolysis or methanolysis, releasing a yellow-colored 4-nitrophenolate ion upon cleavage. This property makes it a useful tool in monitoring enzyme activity and studying the kinetics of esterase and lipase enzymes.

Uses

Used in Enzyme Activity Assays:
4-Nitrophenyl Acetate is used as a substrate to study the enzymatic activity of Carbonic Anhydrase III isolated from bovine skeletal muscle. The release of the 4-nitrophenolate ion upon hydrolysis allows for the quantification of enzyme activity and provides insights into the enzyme's catalytic properties.
Used in Peptide Chemistry:
In the field of peptide chemistry, 4-Nitrophenyl Acetate is used with iodoacetic acid for the reductive cleavage of methionine-containing peptides. This application aids in the analysis and manipulation of peptide sequences, facilitating the study of protein structure and function.
Used in Esterase and Lipase Assays:
4-Nitrophenyl Acetate serves as a substrate in assays for esterase and lipase activity. The yellow-colored product formed upon hydrolysis allows for the easy detection and quantification of enzyme activity, making it a valuable tool in the study of these enzymes and their potential applications.
Used in Inorganic Complex Evaluation:
In the study of inorganic complexes, 4-Nitrophenyl Acetate is utilized to evaluate the methanolysis or hydrolysis activity of these complexes. The release of the 4-nitrophenolate ion provides a means to assess the catalytic efficiency and selectivity of the inorganic complexes in ester hydrolysis reactions.

Synthesis Reference(s)

Synthesis, p. 991, 1981 DOI: 10.1055/s-1981-29674

Purification Methods

Recrystallise the ester from absolute EtOH [Moss et al. J Am Chem Soc 108 5520 1986]. [Beilstein 6 IV 1298.]

InChI:InChI=1/C8H7NO4/c1-6(10)13-8-4-2-7(3-5-8)9(11)12/h2-5H,1H3

Upstream product

• 24067-17-2 4-nitrophenylboronic acid 
• 3375-31-3 palladium diacetate 
• 14609-74-6 p-nitrophenolate 
• 108-24-7 acetic anhydride 
• 100-19-6 (4-nitrophenyl)ethanone 
• 100-02-7 4-nitro-phenol 
• 155164-63-9 2-acetyl-4,5-dichloropyridazin-3(2H)-one 
• 100-00-5 4-chlorobenzonitrile 
• 104013-15-2 2-phenylpropionic acid p-nitrophenyl ester 
• 321865-45-6 cyclobutanecarboxylic acid 4-nitrophenyl ester 
• 72289-61-3 phenyl-2 butyrate de p-nitrophenyle 
• 26050-99-7 p-nitrophenyl cyclopropanecarboxylate 
• 42721-91-5 4-nitrophenyl cyclopentanecarboxylate 
• 959-22-8 p-nitrophenylbenzoate 

Downstream Products

• 13871-68-6 p-aminophenyl acetate 
• 1450-76-6 1-(2-hydroxy-5-nitrophenyl)ethanone 
• 79030-44-7 4,4'-diacetoxyazoxybenzene 
• 74069-32-2 C₄₂H₇₀O₃₅*C₈H₇NO₄ 
• 100-02-7 4-nitro-phenol 
• 1218-34-4 N-AcTrp 
• 2280-01-5 N-acetyl-D-tryptophan 
• 2824-57-9 N-acetyl-L-tryptophan methyl ester 
• 2824-57-9 AcTrpOMe 
• 587-48-4 3-acetylaminobenzoic acid 
• 14609-74-6 p-nitrophenolate 
• 878-00-2 4-formylphenyl acetate 
• 13031-41-9 4-cyanophenyl acetate 
• 74231-54-2 pyridine-4-carbaldehyde-((E)-O-acetyl oxime ) 

Relevant articles and documents

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Protonic Reorganization in Catalysis by Serine Proteases: Acylation by Small Substrates

The pH (pD)-rate profiles for acylation of α-lytic protease in protium and deuterium oxides by p-nitrophenyl acetate show pK values of 5.92 and 6.60, well below the enzyme ionization pK values of 6.70 and 7.35.This is attributed to a pH-induced change in the rate-determining step.The data are consistent with an initial acylation of active-site histidine (protolytically assisted, kH/kD = 2.4), followed by an intramolecular N -> O acyl shift to active-site serine by parallel specific-acid-catalyzed (kH/kD = 0.5) and general-acid-catalyzed (kH/kD = 2) routes.The magnitude of pK(D2O) - pK(H2O) and a proton inventory of the general-acid-catalyzed N -> O acyl shift both suggest that deprotonation of α-lytic protease generates an unusual protonic site with a "loosely bound" proton.The β-deuterium isotope effect, k3H/k3D = 0.98, for the same step confirms nucleophilic interaction at carbonyl in the transition state.An abbreviated proton inventory for acylation of α-chymotrypsin by p-nitrophenyl acetate is consistent with a "loosely bound" proton there also.A proton inventory for acylation of elastase by N-(carbobenzyloxy)-L-alanine p-nitrophenyl ester is linear, suggesting one-proton catalysis and indicating that if "loosely bound" reactant-state protons are present, they are catalytically silent.The general picture, from this work and that of others, is that the catalytic response of serine proteases to small, "unnatural" substrates is highly variable, both in site of nucleophilic attack and involvement of protolytic catalysis.Probably mutual transition-state interactions over an extended region of both enzyme and natural-substrate structure are required to bring into active function the full catalytic capability with which the serine proteases have been endowed by biological evolution.

Efficient Assay for the Detection of Hydrogen Peroxide by Estimating Enzyme Promiscuous Activity in the Perhydrolysis Reaction

Hydrogen peroxide is an ideal oxidant in view of its availability, atom economy, or green aspects. Furthermore, it is produced by the cell mitochondria and plays a meaningful role in controlling physiological processes, but its unregulated production leads to the destruction of organs. Due to its diverse roles, a fast and selective method for hydrogen peroxide detection is the major limitation to preventing the negative effects caused by its excess. Therefore, we aimed to develop an efficient assay for the detection of H2O2. For this purpose, we combined the enzymatic method for the detection of hydrogen peroxide with the estimation of the promiscuity of various enzymes. We estimated the activity of an enzyme in the reaction of p-nitrophenyl esters with hydrogen peroxide resulting in the formation of peracid. To our knowledge, there is no example of a simple, multi-sensor demonstrating the promiscuous activity of an enzyme and detecting hydrogen peroxide in aqueous media.

PRODRUGS OF THE TYROSINE KINASE INHIBITOR FOR TREATING CANCER

There are provided compounds of Formula (I), and pharmaceutically acceptable salts and esters thereof, and pharmaceutical compositions thereof, useful for inhibition or modulation of the activity of tyrosine kinases and treatment of disease states or conditions mediated by tyrosine kinases, including cancers. (I)