74034-99-4

Usage

Chemical compound

2-amino-4-(4-hydroxyphenyl)-4-oxobutanoic acid

Also known as

Dopastin
Derivative of the amino acid tyrosine
Plays a crucial role in the synthesis of neurotransmitters dopamine, norepinephrine, and epinephrine
Involved in various physiological processes such as mood regulation, stress response, and cognitive function
Contains a hydroxyphenyl group indicating potential antioxidant properties
Important for protecting cells from oxidative damage
Studied for potential therapeutic applications in neurodegenerative disorders and mood-related conditions

Upstream product

• 2632-13-5 2-Bromo-4'-methoxyacetophenone 
• 73994-51-1 2-Acetylamino-2-(p-methoxyphenacyl)-malonsaeure-diaethylester 
• 61172-78-9 D,L-4-Oxo-homotyrosin 
• 73994-54-4 2-(2-Chloro-acetylamino)-4-(4-hydroxy-phenyl)-4-oxo-butyric acid 

Relevant academic research and scientific papers

Fluorescent analogues of the insect neuropeptide helicokinin I: Synthesis, photophysical characterization and biological activity

In insects numerous physiological processes are regulated by neuropeptides. Two fluorescent analogues of the amino acids tryptophan and tyrosine were synthesized and incorporated in the diuretic neuropeptide helicokinin I from the moth Heliothis zea. By fluorescence emission measurements it was shown that both fluorescent helicokinin I analogues react sensitive on the dielectricity of their microenvironment. A helicokinin I analogue containing the fluorescent tryptophan mimic β-[6'-(N,N-dimethyl)-amino-2'-naphthoyl]alanine (Ald) was shown to bind to dodecylphosphocholine (DPC) micelles by the Ald residue. A membrane binding model for helicokinin I is proposed based on data from related mammalian and insect-neuropeptides.

24. Stoffwechselprodukte von Mikroorganismen. Ueber das 4-Oxo-homotyrosin, ein Abbauprodukt des Echinocandins B

D,L-4-Oxo-homotyrosine was synthesized by the acetylaminomalonic ester pathway.The optical resolution was carried out by means of the enzyme acylase I.The L-configuration of the enzymatically produced amino acid was confirmed by degradation to L-aspartic acid. 4-Oxo-homotyrosine obtained by degradation of the polypeptide antibiotic echinocandine B has D-configuration, but his optical purity is low.A hypothetical explanation for its formation from the (2S,3S,4S)-3,4-dihydroxyhomotyrosine residue of echinocandine B is proposed.