300-34-5

Usage

Uses

Used in Pharmaceutical Industry:
3-Amino-L-tyrosine is used as a precursor in the synthesis of pharmaceuticals for its ability to contribute to the production of essential neurotransmitters and its potential role in the development of new drugs targeting dopamine receptors.
Used in Neurodegenerative Disorder Treatment:
3-Amino-L-tyrosine is utilized as a therapeutic agent for neurodegenerative disorders such as Parkinson's disease, due to its potential to enhance dopamine levels and mitigate the effects of these conditions.
Used in Medicinal Chemistry Research:
3-Amino-L-tyrosine serves as a subject of interest in medicinal chemistry research, where it is explored for its antioxidant properties and its capacity to influence neurotransmitter synthesis, offering avenues for the treatment of various neurological conditions.

InChI:InChI=1/C9H12N2O3/c10-6-3-5(1-2-8(6)12)4-7(11)9(13)14/h1-3,7,12H,4,10-11H2,(H,13,14)

Upstream product

• 605-65-2 5-(dimethylamino)naphth-1-ylsulfonyl chloride 
• 621-44-3 3-nitro-L-tyrosine 
• 60-18-4 L-tyrosine 

Downstream Products

• 127290-64-6 α-D-L-3-aminotyrosine 
• 127290-64-6 C₉H₁₁⁽²⁾HN₂O₃ 
• 725726-11-4 2,2,3,3,4,4,4-Heptafluoro-butyric acid 2-(2,2,3,3,4,4,4-heptafluoro-butyrylamino)-4-[(S)-2-(2,2,3,3,4,4,4-heptafluoro-butyrylamino)-3-(2,2,3,3,4,4,4-heptafluoro-butyryloxy)-3-oxo-propyl]-phenyl ester 
• 96844-03-0 3-(3-cyano-4-hydroxyphenyl)-L-alanine 
• 685878-63-1 C₉H₁₀N₂O₃ 

Relevant academic research and scientific papers

Conversion of a Dehalogenase into a Nitroreductase by Swapping its Flavin Cofactor with a 5-Deazaflavin Analogue

Natural and engineered nitroreductases have rarely supported full reduction of nitroaromatics to their amine products, and more typically, transformations are limited to formation of the hydroxylamine intermediates. Efficient use of these enzymes also requires a regenerating system for NAD(P)H to avoid the costs associated with this natural reductant. Iodotyrosine deiodinase is a member of the same structural superfamily as many nitroreductases but does not directly consume reducing equivalents from NAD(P)H, nor demonstrate nitroreductase activity. However, exchange of its flavin cofactor with a 5-deazaflavin analogue dramatically suppresses its native deiodinase activity and leads to significant nitroreductase activity that supports full reduction to an amine product in the presence of the convenient and inexpensive NaBH4.

A derivatization assay using gaschromatography/negative chemical ionization tandem mass spectrometry to quantify 3-nitrotyrosine in human plasma

Endogenous free or protein-associated 3-nitrotyrosine (3-NT) has been proposed as a biomarker of in vivo oxidative damage caused by nitrating agents. Isotopic dilution assay gaschromatographic/mass spectrometric (GC/MS) techniques have been employed to measure endogenous 3-NT levels. However, the quantitative normal plasma values reported so far are inconsistent. The results vary between the assays; they may have been influenced by in vitro artifactual nitration of tyrosine to 3-NT. In this study, a simple and artifact-free derivatization method for quantifying the endogenous 3-NT content of biological samples by GC/negative chemical ionization MS/MS is presented. The method is based on reduction of the nitro group of the molecule by dithionite, heptafluorobutyric acylation and subsequent methyl derivatization, di-O-methyldi-N-heptafluorobutyryl being the major derivative. The results showed excellent GC and MS properties, such as low background and a favorable fragmentation pattern. Endogenous 3-NT was unequivocally quantified using collision-induced dissociation in the selected reaction monitoring mode, whereas co-elution of unknown compounds interfered in the selected-ion monitoring mode. We found that tyrosine was nitrated in the presence of nitrate anions and heptafluorobutyric anhydride, but the product appeared as a di-O-methylmono-N-heptafluorobutyryl derivative. Therefore, artifactually formed 3-NT did not contribute to the measured endogenous 3-NT level owing to its different derivative structure. The method was applied to determine endogenous 3-NT in human plasma and plasma proteins. A detection limit of 0.03 nm for 13C6-labeled 3-NT in plasma samples was established and the response was linear over a concentration range of 0-50 nM (R2 > 0.999). The endogenous free 3-NT level (mean ± SD) in ultrafiltered plasma samples from 12 healthy adults was 0.74 ± 0.30 nM. The mean concentration of 3-NT in their plasma total proteins was 0.60 ± 0.40 pmol mg-1. Hence, the described method is selective, eliminates the problem of artifactual nitration and is feasible for the quantification of free and protein-associated 3-NT in biological samples such as plasma. Copyright