2360-97-6

Basic information

• Product Name: H-PHE-PNA HCL
• Synonyms: H-PHE-PNA HCL;H-L-PHE-PNA;L-PHENYLALANINE-P-NITROANILIDE;L-PHENYLALANINE 4-NITROANILIDE;L-PHENYLALNINE-P-NITROANILIDE;L-Phenylalanine 4-nitroanilide45 / 5g;H-L-Phe-pNA*HCl;L-Phenylalnine-p-nitroanilide hydrochloride
• CAS NO: 2360-97-6
• Molecular Formula: C₁₅H₁₅N₃O₃
• Molecular Weight: 321.76
• Mol File: 2360-97-6.mol

Chemical Properties

• Boiling Point: 543.036 °C at 760 mmHg
• Flash Point: 282.218 °C
• Appearance: /
• Density: 1.323 g/cm³
• Storage Temp.: -15°C
• Solubility: Chloroform (Slightly), Dichloromethane (Slightly), Methanol (Slightly, Sonicated
• CAS DataBase Reference: H-PHE-PNA HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-PHE-PNA HCL(2360-97-6)
• EPA Substance Registry System: H-PHE-PNA HCL(2360-97-6)

Safety Data

• Safety Statements: S22:Do not inhale dust.; S24/25:Avoid contact with skin and eyes.
• Hazardous Substances Data: 2360-97-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-PHE-PNA HCL is used as a substrate for aminopeptidase M (microsomal alanyl aminopeptidase) for the study and analysis of enzyme activity and function. This application aids in understanding the role of these enzymes in various biological processes and their potential as therapeutic targets.
Used in Research and Development:
H-PHE-PNA HCL is used as a substrate in the study of a novel cytosolic leucyl aminopeptidase. This application helps researchers investigate the properties and functions of these enzymes, which can contribute to the development of new drugs and therapies.
Used in Diagnostics:
H-PHE-PNA HCL can be employed in the development of diagnostic tools and assays to measure the activity of aminopeptidases. This can be useful in the detection and monitoring of various diseases and conditions related to enzyme dysfunction.
Used in Biochemical Education:
As a substrate for enzymatic reactions, H-PHE-PNA HCL can be utilized in educational settings to teach students about enzyme kinetics, mechanisms, and the role of enzymes in biological systems.

Upstream product

• 14235-15-5 benzyl (S)-(1-((4-nitrophenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 61043-41-2 H-Ala-Ala-Phe-p-nirtoanilide 
• 97885-48-8 N-(1,1-dimethylethoxycarbonyl)-L-phenylalanine N-(4-nitrophenyl)amide 
• 100-01-6 4-nitro-aniline 
• 2448-45-5 Cbz-D-Phe 
• 5241-58-7 L-Phenylalanine amide 
• 100-00-5 4-chlorobenzonitrile 
• 586-78-7 para-nitrophenyl bromide 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 

Downstream Products

• 135682-47-2 N-3-carboxy-2-propenoylphenylalanine p-nitroanilide 
• 63276-82-4 benzyloxycarbonylglycyl-glycyl-phenylalanine p-nitroanilide 
• 74569-62-3 N-tert-butyloxyacetylphenylalanine p-nitroanilide 
• 63-91-2 L-phenylalanine 
• 100-01-6 4-nitro-aniline 
• 17682-83-6 N-acetyl-L-phenylalanine-p-nitroanilide 
• 21027-71-4 {[(S)-1-(4-Nitro-phenylcarbamoyl)-2-phenyl-ethylcarbamoyl]-methyl}-carbamic acid benzyl ester 
• 85733-98-8 pyroglutamyl-L-phenylalanine p-nitroanilide 
• 186023-50-7 (S)-3-((S)-2-Amino-3-methyl-butyryl)-2,2-dimethyl-oxazolidine-4-carboxylic acid [(S)-1-(4-nitro-phenylcarbamoyl)-2-phenyl-ethyl]-amide 
• 186023-46-1 ((S)-2-Methyl-1-{(S)-4-[(S)-1-(4-nitro-phenylcarbamoyl)-2-phenyl-ethylcarbamoyl]-oxazolidine-3-carbonyl}-propyl)-carbamic acid 9H-fluoren-9-ylmethyl ester 
• 186023-51-8 ((S)-1-{(S)-2-(4-Methoxy-phenyl)-4-[(S)-1-(4-nitro-phenylcarbamoyl)-2-phenyl-ethylcarbamoyl]-oxazolidine-3-carbonyl}-2-methyl-propyl)-carbamic acid 9H-fluoren-9-ylmethyl ester 
• 225798-63-0 {(S)-1-Methyl-2-[(R)-2-[(S)-1-(4-nitro-phenylcarbamoyl)-2-phenyl-ethylcarbamoyl]-cyclopent-(Z)-ylidene]-ethyl}-carbamic acid tert-butyl ester 
• 2440-62-2 N-(3-carboxypropionyl)-L-phenylalanine p-nitroanilide 

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.

Characterisation of the aminopeptidase from non-germinated winter rape (Brassica napus L.) seeds

Rapeseed plays a crucial role in food and fuel industry. Since aminopeptidases take part in many physiological processes in all organisms, it is important to learn their role and characteristics in economically relevant plants. Extracts of non-germinated winter rape seeds were screened for aminopeptidase activity. Substrate specificity, the influence of pH and temperature, as well as effect of protease inhibitors and chosen metal ions on the aminopeptidase activity were determined. The approximate molecular weight estimated by NATIVE-PAGE and SDS-PAGE electrophoresis was ～60 kDa. The partially purified enzyme as well as the aminopeptidases present in crude extract cleaved preferentially Phe-pNA. The activity profiles toward several substrates were also determined. Maximum activity was observed at pH 6.5 and temperature of 40 °C for Phe-pNA as a substrate. Two visible picks in the pH profile toward Phe-pNA, together with other results (IEF) suggest the presence of more than one aminopeptidase, having similar molecular mass. Much lower activity and broad pH profiles were observed for Leu- and Ala-pNA as substrates.

Synthesis of chiral amino acid anilides by ligand-free copper-catalyzed selective N-arylation of amino acid amides

An atom-economic, practical and cost-effective protocol for synthesis of chiral amino acid anilides via ligand-free copper-catalyzed selective C-N cross coupling of chiral amino acid amides and aryl halides, hetereoaryl halides and a vinyl bromide has been developed. No racemization occurred during the C-N coupling. A plausible mechanism is proposed. Copyright

Creation of an artificial metalloprotein with a Hoveyda-Grubbs catalyst moiety through the intrinsic inhibition mechanism of α-chymotrypsin

An l-phenylalanyl chloromethylketone-based inhibitor equipped with a Hoveyda-Grubbs catalyst moiety was regioselectively incorporated into the cleft of α-chymotrypsin through the intrinsic inhibition mechanism of the protein to construct an artificial organometallic protein. The Royal Society of Chemistry 2012.

Local and tunable n→π* interactions regulate amide isomerism in the peptoid backbone

We report that n→π* interactions are operative in peptoids and play a major role in controlling amide isomerism. These interactions can be tuned using α-chiral amide side chains known to promote peptoid folding. To our knowledge, this is the first report of n→π* interactions between amides in non-prolyl systems. Furthermore, we have characterized an n→π* interaction between backbone carbonyls and side chain aromatic rings that can dramatically stabilize the cis-amides required for peptoid helix formation. The tunability of both types of n→π* interactions in peptoids has significant implications for peptoid folding and could be exploited for the design of new peptoid architectures. Copyright

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.

Purification and Some Properties of a Protease from the Sarcocarp of Musk Melon Fruit

A protease has been purified from sarcocarp of musk melon.Cucumis melo ssp. melo var. reticulatus Naud.Earl's Favourite.The protease was mostly present in the placenta part of the fruit and next in the inside mesocarp.The molecular mass of the enzyme was estimated to be about 62 kDa on SDS-PAGE.The enzyme had a carbohydrate moiety.The optimum pH of the enzyme was 11 at 35 deg C using casein as a substrate.The enzyme was stable between pH 6 and 11.The enzyme was strongly inhibited by diisopropyl fluorophosphate, but was not inhibited by EDTA or cysteine protease inhibitors.From the digestion of Ala-Ala-Pro-X-pNA (X = Phe, Leu, Val, Ala, Gly, Lys, Glu, Pro, and diaminopropionic acid (Dap) substrates the specificity of the protease was found to be approximately broad, but the preferential cleavage sites were C-terminal sites of h)drophobic or acidic amino acid residues at P1 position.It was proved that the enzymatic properties of musk melon protease are similar to those of cucumisin .The enzvme was not inhibited by typical proteinous inhibitors such as STI or ovomucoid.Therefore, this enzyme seems to be a useful protease for the food industries. - Keywords: Cucumis melo; Cucurbitaceae; musk melon; plant protease; serine protease.