537-55-3

Basic information

• Product Name: N-Acetyl-L-tyrosine
• Synonyms: L-TYROSINE, N-ACETYL-;ACETYLTYROSINE;ACETYL-L-TYROSINE;AC-TYR-OH;AC-TYROSINE;N-AC-L-TYR;N-ACETYL-L-TYROSINE;N-ACEYL-L-TYROSINE
• CAS NO: 537-55-3
• Molecular Formula: C₁₁H₁₃NO₄
• Molecular Weight: 223.23
• EINECS: 208-671-3
• Product Categories: Amino Acid;amino;Amino Acid Derivatives;Amino Acids;Tyrosine [Tyr, Y];Ac-Amino Acids;Amino Acids (N-Protected);Biochemistry;Nutritional Supplements;Pharmaceutical Intermediates;N-Acetyl-Amino acid series;Amino acids;Biochemicals Found in Plants;Nutrition Research;Pharmacopoeial Amino AcidsPeptide Synthesis;Amino Acid Derivatives;Amino acidsPharmacopoeia (USP);Pharmacopoeia A-ZPharmacopoeia (USP);Tyrosine
• Mol File: 537-55-3.mol

Chemical Properties

• Melting Point: 149-152 °C(lit.)
• Boiling Point: 364.51°C (rough estimate)
• Flash Point: 275.1 °C
• Appearance: /Crystalline
• Density: 1.2446 (rough estimate)
• Vapor Pressure: 4.07E-12mmHg at 25°C
• Refractive Index: 1.4960 (estimate)
• Storage Temp.: 2-8°C
• Solubility: H2O: soluble25mg/mL
• PKA: 3.15±0.10(Predicted)
• Water Solubility: Soluble in water (25 mg/ml), and ethanol.
• Stability: Stable. Incompatible with strong oxidizing agents.
• BRN: 2697172
• CAS DataBase Reference: N-Acetyl-L-tyrosine(CAS DataBase Reference)
• NIST Chemistry Reference: N-Acetyl-L-tyrosine(537-55-3)
• EPA Substance Registry System: N-Acetyl-L-tyrosine(537-55-3)

Safety Data

• Hazard Codes: Xi
• Statements: 41-36/37/38
• Safety Statements: 26-39-36
• WGK Germany: 3
• F: 10
• TSCA: Yes
• Hazardous Substances Data: 537-55-3(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical and Biomanufacturing Industry:
N-Acetyl-L-tyrosine is used as a cell culture media component for the commercial biomanufacture of therapeutic recombinant proteins and monoclonal antibodies. Its involvement in catecholamine production makes it a valuable addition to the process.
Used in Biochemistry and Molecular Biology Research:
As a tyrosine derivative with a chemical structure similar to that of an amino acid, N-Acetyl-L-tyrosine serves as a model system to study the transfer reactions of tyrosine. These reactions are crucial for energy metabolism, protein synthesis, and metal chelation.
Used in Diagnostics:
N-Acetyl-L-tyrosine may be employed as an indicator to differentiate between neurosyphilis patients and syphilis/non-neurosyphilis patients, aiding in the accurate diagnosis of the condition.
Used in Nutritional Supplements:
Due to its enhanced solubility and stability compared to L-tyrosine, N-Acetyl-L-tyrosine is incorporated into commercial parenteral amino acid formulations such as TrophAmine and Aminosyn-II, providing nutritional support for those who require it.

benefits

N-Acetyl-L-Tyrosine (NALT) plays a necessary part in the synthesis of dopamine and other hormones in your body. It can boost levels of the neurotransmitters dopamine, norepinephrine and epinephrine. It helps to support higher levels of focus and cognitive function. It can increase working memory and feelings of well-being.

Side effects

L-tyrosine gets the generally regarded as safe (GRAS) stamp of approval from the FDA. Some side effects of N-Acetyl-L-tyrosine (NALT) include nausea, headache, fatigue, and heartburn. It can be safely taken for extended periods of time.

InChI:InChI=1/C11H13NO4/c1-7(13)12-10(11(15)16)6-8-2-4-9(14)5-3-8/h2-5,10,14H,6H2,1H3,(H,12,13)(H,15,16)/p-1/t10-/m0/s1

Upstream product

• 840-97-1 N-acetyl-L-tyrosine ethyl ester 
• 2440-79-1 N-acetyl-L-tyrosine methyl ester 
• 108-24-7 acetic anhydride 
• 60-18-4 L-tyrosine 
• 64-17-5 ethanol 
• 23525-90-8 2-acetylamino-3-(4-hydroxyphenyl)propionic acid methyl ester 
• 1948-71-6 N-acetyl-L-tryrosinamide 
• 55264-42-1 glycine amide hydrobromide 
• 64896-33-9 (Z)-2-acetamido-3-(p-hydroxyphenyl)-2-propenic acid 
• 71-23-8 propan-1-ol 
• 60-24-2 2-hydroxyethanethiol 
• 675587-71-0 N^α-acetyl-O-(2,4-dinitro-5-(dimethylaminomethyl)phenyl)-L-tyrosine 
• 934740-76-8 2-acetylamino-3-(4-hydroxy-phenyl)-propionic acid methoxycarbonylmethyl ester 
• 30697-69-9 ethyl N-acetyl-tyrosinate 

Downstream Products

• 17355-24-7 (S)-N-acetyl-3-(4-methoxyphenyl)alanine methyl ester 
• 2440-79-1 N-acetyl-L-tyrosine methyl ester 
• 840-97-1 N-acetyl-L-tyrosine ethyl ester 
• 56186-52-8 N-acetyl-O-(2,4-dinitro-phenyl)-L-tyrosine 
• 2901-77-1 N-acetyltyrosine 
• 60-18-4 L-tyrosine 
• 182002-68-2 4'<(3''-acetyl-5''-oxo-2''-thioxoimidazolidin-4''-yl)methyl>phenyl acetate 
• 388587-63-1 rac-1-O-(N^α-acetyl-L-tyrosinyl)glycerol 

Relevant articles and documents

Unusual Enhancement of Protease Activity in Organic Solvents by Amines

The catalytic activities of subtilisin BPN' and α-chymotrypsin for transesterification of N-acetyl-L-tyrosine methyl ester in organic solvents were dramatically increased by addition of tertiary amines.The effects may be ascribed to the change in dissociation state of polar groups on the surface of the enzymes.

Fluorescence Spectroscopic Study of α-Chymotrypsin as Relevant to Catalytic Activity in Aqueous-Organic Media

The effects of the composition of aqueous-organic mixed solvents on steady state fluorescence emission of α-chymotrypsin were investigated.In all the solvent systems, maximum wavelength of fluorescence emission shifted initially to higher wavelength and then to lower wavelength by increasing water content in organic solvents.The results were interpreted in terms of the changes in microenvironment of tryptophan residues in the enzyme due to conformational modification of the enzyme.The maximoum emission wavelength of chymotrypsin is well correlated to its catalytic activity for the hydrolysis of N-acetyl-L-tyrosine ethyl ester.Activity of chymotrypsin decreased or it was totally inhibited at solvent compositions which give long emission wavelength of the enzyme.The results suggest that the fluorescence spectroscopy may be useful for detection of conformational chnges and alternation of catalytic activity of the enzyme.

Effect of dioxane on the binding of competitive inhibitor proflavin and catalytic activity of bovine pancreatic α-chymotrypsin

The binding of competitive inhibitor proflavin by α-chymotrypsin in water-dioxane mixtures over the entire range of thermodynamic activities of water a w was studied. The data on the degree of binding of proflavin were compared to the results on the catalytic activity of the enzyme preliminary incubated in water-dioxane mixtures. An analysis of the behavior of the concentration dependences of these characteristics demonstrated that, at low a w values, the behavior of the interprotein contacts in the enzyme formed during its drying largely governs its functional properties, while at high a w values, they are determined by the interaction of the enzyme with the organic solvent. Interplay of these two factors is responsible for the observed complex shape of the isotherm of binding of proflavin, with the maximum degree of binding being attained at moderate a w values.

Structure-activity relationship studies of dipeptide-based hepsin inhibitors with Arg bioisosteres

Hepsin is a type II transmembrane serine protease (TTSP) associated with cell proliferation and overexpressed in several types of cancer including prostate cancer (PCa). Because of its significant role in cancer progression and metastasis, hepsin is an attractive protein as a potential therapeutic and diagnostic biomarker for PCa. Based on the reported Leu-Arg dipeptide-based hepsin inhibitors, we performed structural modification and determined in vitro hepsin- and matriptase-inhibitory activities. Comprehensive structure-activity relationship studies identified that the p-guanidinophenylalanine-based dipeptide analog 22a exhibited a strong hepsin-inhibitory activity (Ki = 50.5 nM) and 22-fold hepsin selectivity over matriptase. Compound 22a could be a prototype molecule for structural optimization of dipeptide-based hepsin inhibitors.

GRANZYME B DIRECTED IMAGING AND THERAPY

Provided herein are heterocyclic compounds useful for imaging Granzyme B. Methods of imaging Granzyme B, combination therapies, and kits comprising the Granzyme B imaging agents are also provided.

Photoinduced electron transfer-promoted debenzylation of phenylalanine and tyrosine derivatives using dicyanoarene

Photoinduced debenzylations of phenylalanine and tyrosine derivatives with dicyanoarenes afford glycine derivatives by the generation of radical cations. Despite the limited substrate scope, the radical cation of phenylalanine and tyrosine derivatives bearing both a carbamate (without an aromatic group) at the N-terminal and an amide at the C-terminal could promote the breaking C–C bond at the benzylic position by a photoinduced electron transfer. It is important to understand the chemical behavior of the radical cations of phenylalanine and tyrosine in enzymes involving electron transfer.

Radical arylation of tyrosine residues in peptides

The radical arylation of the phenolic side chain of tyrosine in peptides was investigated. Aryl radicals were generated from aryldiazonium salts using titanium(III) chloride as stoichiometric reductant. Due to the high selectivity with which 3-aryltyrosine derivatives were formed, this reaction type represents a new strategy for the direct functionalization of peptides.

Peptide Tyrosinase Activators

Peptides that increase melanin synthesis are provided. These peptides include pentapeptides YSSWY, YRSRK, and their variants. The peptides may activate the enzymatic activity of tyrosinase to increase melanin synthesis. The pharmaceutical, cosmetic, and other compositions including the peptides are also provided. The methods of increasing melanin production in epidermis of a subject are provided where the methods include administering compositions comprising an amount of one or more peptides effective to increase the melanin production. The methods also include treating vitiligo or other hypopigmentation disorders with compositions including one or more peptides.

Oxidative damage of aromatic dipeptides by the environmental oxidants NO2 and O3

Irreversible oxidative damage at both aromatic side chains and dipeptide linkage occurs in the aromatic N- and C-protected dipeptides 7-11 upon exposure to the environmental pollutants NO2 and O3. The reaction proceeds through initial oxidation of the aromatic ring by in situ generated NO3, or by NO2, respectively, which leads to formation of nitroaromatic products. The indole ring in Phe-Trp undergoes oxidative cyclization to a pyrroloindoline. An important reaction pathway for dipeptides with less oxidisable aromatic side chains proceeds through fragmentation of the peptide bond with concomitant acyl migration. This process is likely initiated by an ionic reaction of the amide nitrogen with the NO2 dimer, N2O4. This journal is

Hydrogen/deuterium exchange of cross-linkable α-amino acid derivatives in deuterated triflic acid

In this paper we report here a hydrogen/deuterium exchange (H/D exchange) of cross-linkable α-amino acid derivatives with deuterated trifluoromethanesulfonic acid (TfOD). H/D exchange with TfOD was easily applied to o-catechol containing phenylalanine (DOPA) within an hour. A partial H/D exchange was observed for trifluoromethyldiazirinyl (TFMD) phenylalanine derivatives. N-Acetyl-protected natural aromatic α-amino acids (Tyr and Trp) were more effective in H/D exchange than unprotected ones. The N-acetylated TFMD phenylalanine derivative afforded slightly higher H/D exchange than unprotected derivatives. An effective post-deuteration method for cross-linkable α-amino acid derivatives will be useful for the analysis of biological functions of bioactive peptides and proteins by mass spectrometry.