840-97-1

Usage

Enzyme inhibitor

This ester (FW = 251.28 g/mol; Abbreviation ATEE) is a substrate for chymotrypsin that is frequently used in assays of that enzyme. The reaction can be followed by observing the production of free carboxyl groups or by the decrease in absorbance at 237 nm and pH 7. Supersaturated stock solutions (i.e., 10-20 mM) can be prepared by dissolving ATEE in water at 85°C, followed by rapidly cooling to room temperature. These solutions are typically stable for six to twelve hours. N-Acetyl-L-tyrosine ethyl ester inhibits protein-disulfide reductase, glutathione-requiring; thiolsubtilisin; complement component C’.

InChI:InChI=1/C13H17NO4/c1-3-18-13(17)12(14-9(2)15)8-10-4-6-11(16)7-5-10/h4-7,12,16H,3,8H2,1-2H3,(H,14,15)/t12-/m1/s1

Upstream product

• 64-17-5 ethanol 
• 537-55-3 N-acetyl-L-tyrosine 
• 2440-79-1 N-acetyl-L-tyrosine methyl ester 
• 2361-96-8 ethyl N-acetyl-(L)-phenylalaninate 
• 537-55-3 N-acetyl-L-tyrosine 
• 75-36-5 acetyl chloride 
• 60-18-4 L-tyrosine 
• 949-67-7 L-tyrosine ethyl ester 
• 108-24-7 acetic anhydride 

Downstream Products

• 1948-71-6 N-acetyl-L-tryrosinamide 
• 537-55-3 N-acetyl-L-tyrosine 
• 2381-07-9 N-acetyltyrosine hydrazide 
• 29739-71-7 N-acetyl-L-tyrosine propyl ester 
• 127132-50-7 N-acetyl-O'-(but-3-enyl)-L-tyrosine ethyl ester 
• 126530-19-6 acetyltyrozine-glycyl-leucine 
• 126530-20-9 Ac-Tyr-Gly-Leu-Gly-Leu 
• 126530-21-0 Ac-Tyr-Gly-Gly-Leu 
• 23506-48-1 N-Ac-L-Tyr-Gly-Gly 
• 126530-15-2 acetyltyrosyl-threonine amide 
• 126530-22-1 Ac-Tyr-Gly-Phe-Leu 
• 141215-12-5 N-Ac-L-Tyr-Gly-GlyOEt 
• 81543-10-4 Ac-Tyr-Gly-Gly-NH₂ 
• 65356-76-5 N-Ac-L-Tyr-L-Leu-NH₂ 

Relevant academic research and scientific papers

Time-dependent structure and activity changes of alpha-chymotrypsin in water/alcohol mixed solvents.

Secondary structure of alpha-chymotrypsin in water/ethanol was investigated by circular dichroic (CD) spectroscopy. The changes in catalytic activity were discussed in terms of structural changes of the enzyme. Alpha-chymotrypsin formed beta-sheet structure in water/ethanol (50/50 by volume), but it was substantially less active as compared to that in water. At water/ethanol 10/90, alpha-chymotrypsin took on a native-like structure, which gradually changed to beta conformation with concomitant loss of activity. Change of solvent composition from water/ethanol 50/50 to 90/10 or 10/90 by dilution with water or ethanol, respectively, led to partial recovery of native or native-like structure and activity. In water/methanol, alpha-chymotrypsin tended to form stable beta-sheet structure at water/methanol ratios lower than 50/50, but the catalytic activity decreased with time. Change to alpha-helix structure with substantial loss in catalytic activity was observed when alpha-chymotrypsin was dissolved in water/2,2,2-trifluoroethanol with water contents lower than 50%. In water/2,2,2-trifluoroethanol 90/10, alpha-chymotrypsin initially had the CD spectrum of native structure, but it changed with time to that characteristic of beta-sheet structure.

Visible-Light Mediated Tryptophan Modification in Oligopeptides Employing Acylsilanes

A method for the selective tryptophan modification and labelling of tryptophan-containing peptides is described. Photoirradiation of acylsilanes generates reactive siloxycarbenes which undergo H?N-insertion into the indole moiety of tryptophan to give stable silyl protected hemiaminals. This method is successfully applied to chemically modify various tryptophan containing oligopeptides. The method enables the selective introduction of alkynes to peptides that are eligible for further alkyne-azide click chemistry. In addition, the dansyl fluorophore can be conjugated to a peptide using this approach.

Preparation method of rosastat key intermediate

The invention provides a preparation method of a rosastat key intermediate. The intermediate I is 4-hydroxy-1-methyl-7-phenoxy isoquinoline-3-carboxylic ester. The preparation method comprises the following steps: with tyrosine as an initial raw material, sequentially carrying out esterification, acylation, etherification, cyclization, aromatization and oxidation rearrangement reaction to preparethe rosastat key intermediate. The preparation method has the advantages of cheap and easily available raw materials, environmental protection, avoiding of use of phosphorus oxychloride, polyphosphoric acid and other environmentally unfriendly reagents in the cyclization reaction, simple process, simple operation and mild reaction conditions; and the method has the advantages of less three wastesand higher product yield and purity, and is suitable for industrial production.

Resolution of N-protected amino acid esters using whole cells of Candida parapsilosis ATCC 7330

Whole cells of Candida parapsilosis ATCC 7330 were used for the resolution of N-acetyl amino acid esters. Excellent enantioselectivities (E = 40 to >500) were achieved for the resolution of N-protected protein and non-protein amino acid esters giving good yields (28-50%) and high enantiomeric excesses (up to >99%) for both enantiomers.

Synthesis and evaluation of N-acetyl-l-tyrosine based compounds as PPARα selective activators

The development of type 2 diabetes in obese individuals is linked to lipid accumulation in non-adipose tissues. A series of N-acetyl-l-tyrosine derivatives were synthesized and evaluated for PPAR transactivation. Compounds 4d and 4f were found to show better PPARα transactivation as compared to PPARγ. Molecular docking analysis was carried out to study their important interactions with the active site of PPARα.

Process for preparation of tamsulosin and its aralkylamine derivatives

The present invention discloses a new process for the synthesis of tamsulosin and its aralkylamine derivatives, especially (R)-(?)-5-{2-[2-(2-alkoxyphenoxy)ethylamino]propyl}-2-alkoxybenzenesulfonamides having the following formula 1 (where R1 and R2 represent C1-C4 alkyl groups) and their hydrochloride thereof, and other various pharmaceutical used salts. Tamsulosin hydrochloride (R1=Et, R2=Me, in its hydrochloride salt form) is an antagonist of α-A adrenoceptors in the prostate. Tamsulosin?HCl occurs as white crystals, which melt with decomposition at approximately 230° C. It is sparingly soluble in water and in methanol, slightly soluble in glacial acetic acid and in ethanol, and practically insoluble in ether.

Process for preparation of tamsulosin and its derivatives

The present invention discloses a new process for the synthesis of tamsulosin derivatives of formula 1 (where R 1 and R 2 represent C 1 -C 4 alkyl groups) and their hydrochlorides and other pharmaceutically acceptable salts, comprising reacting the hydrochloride of sulphonamide 2 (where R represents C 1 -C 4 alkyl) with the ether compound 21 (where R' represents C 1 -C 4 alkyl and R" represents MeC 6 H 4 SO 2 or MeSO 2 ).

Effects of metal salts on the structure and activity of α-chymotrypsin in ethanol/water

The catalytic activity and circular dichroic (CD) spectra of α- chymotrypsin (CT) were measured in ethanol/water (95/5, v/v) solution containing small amounts of metal salts. Although the catalytic activity of CT increased upon the addition of all the metal salts used, the magnitude of activity increase was different for different metal salts. Especially, calcium acetate accelerated the transesterification of amino acid up to 6 fold at 100 μM. The secondary and tertiary structures of CT were also changed by metal salts, as studied by CD measurements. The effects of metal salts on the stability of CT in ethanol/water were also studied, and it was found that the residual activity of CT after 7 days in ethanol/water in the presence of Ca(OCOCH3)2 was about 20% of the initial activity. The change in activity was closely correlated with the change in the mean residue ellipticity of CT at 208 or 230 nm.

Increase of catalytic activity of alpha-chymotrypsin by metal salts for transesterification of an amino acid ester in ethanol.

alpha-Chymotrypsin-catalyzed transesterification of N-acetyl-L-tyrosine methyl ester in ethanol was markedly accelerated by addition of small amounts of divalent metal salts. The reaction rate dependent not only on the nature of metal ions but also on the nature of anionic counter ions. Calcium acetate was the most effective among the metal salts used. The reaction followed Michaelis-Menten kinetics, and it was found that the reaction increase is due to the increase in kcat.

Concentration- and Structure-Dependent Effects of Amides on Protease Activity in Organic Solvents

The catalytic activity of α-chymotrypsin (CT) in the transesterification of N-acetyl-L-tyrosine methyl ester to its ethyl ester in aqueous-organic media was markedly enhanced by replacing a part of water with foramide.The activity of CT was strongly dependent on the formamide/water ratio, and excess formamide retarded the activity.Addition of formamide to reaction mixtures at constant water contents exhibited similar activation-deactivation profiles for CT.A kinetic study revealed that the rate acceleration is due to an increase in kcat rather than a change in Km.At a given concentration of amides (0.5 M, M = mol dm-3), propionamide and DMF were much less effective than formamide for activation of CT.The results suggest that foramide interacts with CT in a different way from water.