4178-93-2

Usage

Uses

Used in Biochemical Research:
H-LEU-PNA is used as a substrate for the colorimetric determination of leucine aminopeptidase, an enzyme that plays a crucial role in the breakdown of proteins. This application allows researchers to study the activity and regulation of leucine aminopeptidase, which can be useful in understanding its role in various biological processes and potential therapeutic targets.
Used in Pharmaceutical Development:
As an inhibitor, H-LEU-PNA is employed in the development of drugs targeting specific enzymes or proteins. By blocking the activity of these enzymes or proteins, H-LEU-PNA can help researchers understand their function and potential as therapeutic targets for various diseases. This application is particularly relevant in the development of targeted therapies for conditions such as cancer, where inhibiting specific enzymes or proteins can help slow down or stop tumor growth.
Used in Drug Delivery Systems:
H-LEU-PNA's crystalline nature and specific interactions with enzymes and proteins make it a promising candidate for use in drug delivery systems. By incorporating H-LEU-PNA into these systems, researchers can potentially improve the delivery, bioavailability, and therapeutic outcomes of various drugs, particularly those targeting specific enzymes or proteins.

InChI:InChI=1/C12H17N3O3/c1-8(2)7-11(13)12(16)14-9-3-5-10(6-4-9)15(17)18/h3-6,8,11H,7,13H2,1-2H3,(H,14,16)/p+1/t11-/m0/s1

Upstream product

• 1174-27-2 Z-L-Leu-pNA 
• 114684-52-5 N-tert-butoxycarbonyl-L-leucine p-nitroanilide 

Downstream Products

• 123529-88-4 benzyloxycarbonylleucyl-leucine p-nitroanilide 
• 126789-59-1 N-tert-butyloxycarbonylglycyl-L-phenylalanyl-L-leucine p-nitroanilide 
• 100-01-6 4-nitro-aniline 
• 61-90-5 L-leucine 
• 61043-33-2 Z-Ala-Ala-Leu-pNA 
• 216494-70-1 (S)-2-Hydroxy-hexanoic acid [(S)-3-methyl-1-(4-nitro-phenylcarbamoyl)-butyl]-amide 
• 85698-07-3 H-Leu-Leu-pNA*HCl 
• 85697-85-4 Boc-Tyr-Leu-Leu-pNA 
• 82155-59-7 Suc-Tyr-Leu-Leu-pNA 
• 85697-93-4 H-Tyr-Leu-Leu-pNA*HCl 
• 81928-67-8 leucyl-leucine p-nitroanilide 
• 111607-87-5 N-acetylleucyl-leucyl-L-leucine p-nitroanilide 
• 3303-55-7 L-Phe-Leu 
• 14486-16-9 L-Met-L-Leu 

Relevant academic research and scientific papers

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.