154844-41-4

Usage

Uses

Used in Pharmaceutical Research:
Tert-butyl (E)-3-pyrimidin-5-ylprop-2-enoate is used as a key intermediate in the synthesis of various pharmaceutical compounds for its potential to contribute to the development of new drug candidates. Its unique structure, including the pyrimidine ring and the conjugated double bond, may offer specific biological activities that are valuable in medicinal chemistry.
Used in Organic Synthesis:
In the field of organic synthesis, tert-butyl (E)-3-pyrimidin-5-ylprop-2-enoate serves as a versatile building block for the creation of a wide range of organic molecules. Its reactivity, stemming from the presence of the conjugated double bond, allows for various chemical reactions that can be harnessed to produce complex organic compounds.
Used in Agricultural Applications:
Although not extensively detailed in the provided materials, tert-butyl (E)-3-pyrimidin-5-ylprop-2-enoate may also be utilized in agricultural settings. Its potential applications could include the development of agrochemicals, such as pesticides or herbicides, where its chemical properties might offer novel modes of action or enhanced efficacy.
Used in Industrial Settings:
Similarly, in industrial applications, tert-butyl (E)-3-pyrimidin-5-ylprop-2-enoate could be employed in the production of specialty chemicals or materials, where its unique structural features might provide advantages in terms of performance or function.
Further research and testing are essential to fully understand the properties and potential applications of tert-butyl (E)-3-pyrimidin-5-ylprop-2-enoate, ensuring that its use is optimized across various industries.

Upstream product

• 4595-59-9 5-bromopyrimidine 
• 1663-39-4 tert-Butyl acrylate 

Downstream Products

• 154844-42-5 3-Benzyloxycarbonylamino-3-pyrimidin-5-yl-propionic acid tert-butyl ester 
• 309296-08-0 β-(5-Pyrimidinyl)-L-alanine 
• 40929-53-1 β-(5-Pyrimidinyl)acrylic acid 

Relevant academic research and scientific papers

Phenylalanine ammonia-lyase: The use of its broad substrate specificity for mechanistic investigations and biocatalysis - Synthesis of L-arylalanines

Several fluoro-and chlorophenylalanines were found to be good substrates of phenylalanine ammonialyase (PAL/EC 4.3.1.5) from parsley. The enantiomerically pure L-amino acids were obtained in good yields by reaction of the corresponding cinnamic acids with 5M ammonia solution (buffered to pH 10) in the presence of PAL. The kinetic constants for nine different fluoro-and chlorophenylalanines do not provide a rigorous proof for but are consistent with the previously proposed mechanism comprising an electrophilic attack of the methylidene-imidazolone cofactor of PAL at the aromatic nucleus as a first chemical step. In the resulting Friedel-Crafts-type σ complex the β-protons are activated for abstraction and consequently the pro-S is abstracted by an enzymic base. Results from semi-empirical calculations combined with a proposed partial active site model showed a correlation between the experimental kinetic constants and the change in polarization of the pro-S Cβ-H bond and heat of formation of the σ complexes, thus making the electrophilic attack at the neutral aromatic ring plausible. Furthermore, while 5-pyrimidinylalanine was found to be a moderately good substrate of PAL, 2-pyrimidinylalanine was an inhibitor.

Synthesis of Heterocyclic β-Amino Acids. A Convenient Preparation of β-Amino-5-Pyrimidinepropanoic Acid and Derivatives.

The novel (2E)-1,1-dimethylethyl-3-(5-pyrimidinyl)-2-propenoate 3, obtained by Heck coupling between 5-bromopyrimidine and tert-butyl acrylate undergoes nearly quantitative Michael addition in t-butanol saturated with ammonia to the hitherto unknown β-amino-5-pyrimidinepropanoic ester 4.The synthetic utility of this reactions sequence is demonstrated by preparation of 4 on a multigram scale.The transformation of the ester to the free amino acid 5 and to the Cbz-N-protected amino acid 7 is described.The tert-butyl ester 4 and N-protected β-amino acid 7 are useful in peptide and peptidomimic synthesis.