26432-41-7

Upstream product

• 109728-95-2 N,N-phthaloyl-DL-alanine-(4-nitro-anilide) 
• 52299-14-6 N-succinyl-L-alanyl-L-alanyl-L-alanine 4-nitroanilide 
• 1168-86-1 benzyl (S)-(1-((4-nitrophenyl)amino)-1-oxopropan-2-yl)carbamate 
• 52815-81-3 t-butoxycarbonyl-L-alanine p-nitroanilide 

Downstream Products

• 100-01-6 4-nitro-aniline 
• 302-72-7 rac-Ala-OH 
• 85697-77-4 N-Boc-L-Leu-L-Ala-pNA 
• 111195-98-3 ((S)-1-{(S)-3-Methyl-1-[(S)-1-(4-nitro-phenylcarbamoyl)-ethylcarbamoyl]-butylcarbamoyl}-ethyl)-carbamic acid benzyl ester 
• 111196-00-0 ((S)-3-Methyl-1-{(S)-3-methyl-1-[(S)-1-(4-nitro-phenylcarbamoyl)-ethylcarbamoyl]-butylcarbamoyl}-butyl)-carbamic acid benzyl ester 
• 97986-02-2 ({(S)-1-[(S)-1-(4-Nitro-phenylcarbamoyl)-ethylcarbamoyl]-ethylcarbamoyl}-methyl)-carbamic acid benzyl ester 
• 52357-40-1 Z-Ala-Ala-Ala-pNA 
• 111195-99-4 ((S)-3-Methyl-1-{(S)-1-[(S)-1-(4-nitro-phenylcarbamoyl)-ethylcarbamoyl]-ethylcarbamoyl}-butyl)-carbamic acid benzyl ester 
• 111196-05-5 (2-{2-[(S)-1-(4-Nitro-phenylcarbamoyl)-ethylcarbamoyl]-ethylcarbamoyl}-ethyl)-carbamic acid benzyl ester 
• 111195-97-2 [(S)-1-({[(S)-1-(4-Nitro-phenylcarbamoyl)-ethylcarbamoyl]-methyl}-carbamoyl)-ethyl]-carbamic acid benzyl ester 
• 111196-03-3 benzyloxycarbonylalanyl-β-alanyl-alanine p-nitroanilide 
• 117507-16-1 Z-Val-Ala-Ala-pNA 
• 125402-93-9 (S)-2-Amino-N-(4-nitro-phenyl)-propionamide; compound with benzotriazol-1-ol 
• 111196-01-1 benzyloxycarbonylglycyl-prolyl-alanine p-nitroanilide 

Relevant academic research and scientific papers

Proline-based dipeptides with two amide units as organocatalyst for the asymmetric aldol reaction of cyclohexanone with aldehydes

A series of proline-based dipeptide organocatalysts with two amide units (1-16) have been developed and evaluated in the direct catalytic asymmetric aldol reactions of aldehydes with cyclohexanone. These catalysts showed good solubility in organic solvents compared with their corresponding carboxyl terminal dipeptides. The robust amide bond formation allowed structural modifications and fine tuning of catalyst properties by varying the stereo and electronic effects of the terminal amide to affect the ability of hydrogen bonding formation between the catalysts and the substrates. The reactions proceeded smoothly in high yields (up to 99%), enantioselectivities (up to 98% ee) and anti-diastereoselectivities (up to 99:1) in the presence of bifunctional organocatalyst 4 under the optimal reaction conditions.

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.