1991-83-9

Basic information

• Product Name: 4-nitrophenylalanine
• Synonyms: 4-Nitrophenylalanine; NSC 148865; p-Nitrophenylalanine; Phenylalanine, 4-nitro-
• CAS NO: 1991-83-9
• Molecular Formula: C₉H₁₀N₂O₄
• Molecular Weight: 0
• Mol File: 1991-83-9.mol
• Article Data: 11

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 4-nitrophenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: 4-nitrophenylalanine(1991-83-9)
• EPA Substance Registry System: 4-nitrophenylalanine(1991-83-9)

Safety Data

• Hazardous Substances Data: 1991-83-9(Hazardous Substances Data)

Usage

Description

4-nitrophenylalanine is a chemical compound derived from the amino acid phenylalanine, featuring a nitro group at the 4-position of the phenyl ring. This derivative is widely utilized in biochemical and protein research due to its unique chemical structure and properties, which facilitate the study of protein folding, stability, and interactions.

Uses

Used in Biochemical Research:
4-nitrophenylalanine is used as a research tool for studying protein folding and stability, as its chemical structure allows for the investigation of these processes in a controlled manner.
Used in Protein Interaction Analysis:
4-nitrophenylalanine is used as a probe to analyze enzyme activity and protein-protein interactions, providing insights into the mechanisms of these biological processes.
Used in Synthesis of Labeled Peptides and Proteins:
4-nitrophenylalanine is used as a substrate for the synthesis of labeled peptides and proteins, which are valuable for studying biological systems and can be used in various applications such as diagnostics and therapeutics.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 4-nitrophenylalanine is used as a building block for the development of novel drugs, particularly those targeting protein-related diseases, due to its ability to modulate protein function and interactions.
Used in Diagnostics:
4-nitrophenylalanine is used in the development of diagnostic tools, where its incorporation into labeled peptides and proteins can aid in the detection and monitoring of diseases at the molecular level.

InChI:InChI=1/C9H10N2O4/c10-8(9(12)13)5-6-1-3-7(4-2-6)11(14)15/h1-4,8H,5,10H2,(H,12,13)

Upstream product

• 619-89-6 p-nitrocinnamic acid 
• 1627100-31-5 (S)-2-acetamido-3-[²H]-3(4-nitrophenyl)propanoic acid 
• 1627100-30-4 (R)-2-amino-3[(S)-²H]-3(4-nitrophenyl)propanoic acid hydrochloride 
• 1627099-66-4 (S)-methyl 2-acetamido-3-[2H]-3(4-nitrophenyl)propanoate 
• 1627099-40-4 (R)-methyl 2-acetamido-3[2H]-3(4-nitrophenyl)propanoate 
• 1627098-43-4 [4-²H]-methyl 2-acetamido-3(4-nitrophenyl)acrylate 
• 1627096-62-1 [4-²H]-4(4-nitrobenzylidene)-2-methyloxazol-5(4H)-one 
• 94781-50-7 α-deuterio-4-nitro-benzaldehyde 
• 122-04-3 4-nitro-benzoyl chloride 
• 1627101-69-2 (R)-2-amino-3[(R)-²H]-3(4-nitrophenyl)propanoic acid hydrochloride 
• 56613-61-7 (R)-4-nitro-phenylalanine 
• 949-99-5 4-nitro-3-phenyl-L-alanine 
• 882-06-4 4-nitro-trans-cinnamic acid 
• 63-91-2 L-phenylalanine 

Downstream Products

• 6949-60-6 N-formyl-4-nitro-phenylalanine 
• 85317-52-8 methyl 2-amino-3-(4-nitrophenyl)propionate 
• 326019-69-6 dichloroacetic acid-[(R or S)-1-hydroxymethyl-2-(4-nitro-phenyl)-ethylamide] 
• 89288-22-2 2-amino-3-(4-nitrophenyl)propan-1-ol 
• 99861-15-1 N-acetyl-4-amino-3,5-diiodo-phenylalanine 
• 68319-36-8 N-acetyl-4-amino-phenylalanine 
• 29553-99-9 N-acetyl-4-acetylamino-phenylalanine 
• 59515-83-2 4-amino-3,5-diiodo-phenylalanine 
• 106943-05-9 N-[1-(4-Amino-benzyl)-3,3,3-trifluoro-2-oxo-propyl]-benzamide; hydrochloride 
• 106942-39-6 4-(4-Nitro-benzyl)-2-phenyl-4-(2,2,2-trifluoro-acetyl)-4H-oxazol-5-one 
• 106746-00-3 N-[3,3,3-Trifluoro-2-oxo-(4-nitrophenylmethyl)propyl]benzamide 

Relevant articles and documents

Self-assembling behaviour of a modified aromatic amino acid in competitive medium

Aromatic amino acid, specifically phenylalanine (Phe), is one of the most studied building blocks in peptide synthesis due to its importance in biology. It is reported in the literature that Phe-containing peptides have a high tendency to form different self-assembled materials due to efficient aromatic-aromatic interactions. In this article, we have tuned the supramolecular interactions of phenylalanine by making it electron-deficient upon introduction of the nitro group in the ring. The presence of the nitro group has a profound influence on the self-assembly process. It has been observed that 4-nitrophenylalanine (4NP) is a highly efficient gelator compared with the native phenylalanine in DMSO solvent in terms of minimum gelation concentration and it forms hydrogen bonding mediated crystals in water. The change of self-assembling patterns of 4NP in these solvents was studied using X-ray diffraction, UV-Vis spectroscopy, FE-SEM and other techniques. With the help of different experimental data and density functional theory (DFT), we have simulated the theoretical structure of 4NP in DMSO. The theoretical structure of 4NP in DMSO is different compared with that of crystals in water. We then studied the self-assembly process of 4NP in the mixed solvent of DMSO (polar aprotic) and water (polar protic). Different competitive non-covalent interactions of solvents as well as the ratio of the solvent mixture guide the final self-assembly state of 4NP. This journal is

Bi-enzymatic Conversion of Cinnamic Acids to 2-Arylethylamines

The conversion of carboxylic acids, such as acrylic acids, to amines is a transformation that remains challenging in synthetic organic chemistry. Despite the ubiquity of similar moieties in natural metabolic pathways, biocatalytic routes seem to have been overlooked for this purpose. Herein we present the conception and optimisation of a two-enzyme system, allowing the synthesis of β-phenylethylamine derivatives from readily-available ring-substituted cinnamic acids. After characterisation of both parts of the reaction in a two-step approach, a set of conditions allowing the one-pot biotransformation was optimised. This combination of a reversible deaminating and irreversible decarboxylating enzyme, both specific for the amino acid intermediate in tandem, represents a general method by which new strategies for the conversion of carboxylic acids to amines could be designed.

Phenylalanine ammonia lyase catalyzed synthesis of amino acids by an MIO-cofactor independent pathway

Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E1cB elimination mechanism. All manner of things: A competing MIO-independent (MIO=4-methylideneimidazole-5-one) reaction pathway has been identified for phenylalanine ammonia lyases (PALs), which proceeds in a non-stereoselective manner, resulting in the generation of D-phenylalanine derivatives. The mechanism of D-amino acid formation is explored through isotopic-labeling studies and mutagenesis of key active-site residues.