840-97-1

Basic information

• Product Name: N-ACETYL-L-TYROSINE ETHYL ESTER
• Synonyms: N-ALPHA-ACETYL-L-TYROSINE ETHYL ESTER;N-ACETYL-L-TYR ETHYL ESTER;N-ACETYL-L-TYROSINE ETHYL ESTER;ethyln-alpha-acetyl-tyrosinate;ATEE;ETHYLACETYL-L-TYROSINE;AC-TYR-OET;AC-TYROSINE-OET
• CAS NO: 840-97-1
• Molecular Formula: C₁₃H₁₇NO₄
• Molecular Weight: 251.28
• EINECS: 212-663-5
• Product Categories: Amino Acids;Amino Acid Ethyl Esters;Amino Acids (C-Protected);Ac-Amino Acids;Amino Acids (N-Protected);Biochemistry
• Mol File: 840-97-1.mol
• Article Data: 17

Chemical Properties

• Melting Point: 78-81 °C
• Boiling Point: 394.43°C (rough estimate)
• Flash Point: 234.7 °C
• Appearance: /
• Density: 1.1667 (rough estimate)
• Vapor Pressure: 3.03E-09mmHg at 25°C
• Refractive Index: 22 ° (C=1, EtOH)
• Storage Temp.: 2-8°C
• PKA: 9.75±0.15(Predicted)
• Water Solubility: 3.48g/L(28 oC)
• CAS DataBase Reference: N-ACETYL-L-TYROSINE ETHYL ESTER(CAS DataBase Reference)
• NIST Chemistry Reference: N-ACETYL-L-TYROSINE ETHYL ESTER(840-97-1)
• EPA Substance Registry System: N-ACETYL-L-TYROSINE ETHYL ESTER(840-97-1)

Safety Data

• Safety Statements: 24/25
• WGK Germany: 3
• F: 10-21
• Hazardous Substances Data: 840-97-1(Hazardous Substances Data)

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

Downstream Products

• 29701-42-6 N^α-acetyl-S-Tyr-S-AlaNH2 
• 126530-21-0 Ac-Tyr-Gly-Gly-Leu 
• 213549-92-9 (+)-O-diethylphosphino-ethyl ester 
• 29701-41-5 Ac-Tyr-Gly-NH₂ 
• 127132-48-3 ethyl (2S)-2-acetamido-3-(4-allyloxyphenyl)propanoate 
• 19641-91-9 N-acetyl-3,4-dihydroxyphenylalanine ethylester 
• 949-67-7 L-tyrosine ethyl ester 
• 126530-18-5 Ac-Tyr-Glu-NH₂ 
• 537-55-3 N-acetyl-L-tyrosine 
• 124731-84-6 N-acetyltyrosine isopropyl ester 
• 126530-16-3 Ac-Tyr-Tyr-NH₂ 
• 126530-17-4 Ac-Tyr-Arg-NH₂ 
• 126530-14-1 Ac-Tyr-Met-NH₂ 
• 81543-13-7 Ac-Tyr-Gly-Gly-Gly-NH₂ 

Relevant articles and documents

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.

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.

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.