454685-88-2

Usage

Uses

Used in Pharmaceutical and Medicinal Chemistry:
1H-Pyrrolo[2,3-d]pyrimidine-5-carbonitrile (9CI) is used as a building block in the synthesis of organic compounds for its ability to modulate biological processes. It serves as a starting material for the development of pharmaceutical drugs due to its potential to interact with biological targets.
Used in Research and Drug Discovery:
1H-Pyrrolo[2,3-d]pyrimidine-5-carbonitrile (9CI) is utilized as a research tool in the study of biological systems and drug discovery. Its unique structure and properties make it valuable for exploring new avenues in medicinal chemistry and potentially uncovering additional uses and properties through further research and development.

Upstream product

• 271-70-5 7H-pyrrolo[2,3-d]pyrimidine 
• 175791-53-4 5-Iodopyrrolo<2,3-d>pyrimidine 
• 1413065-74-3 5-iodo-7-tosyl-7H-pyrrolo[2,3-d]pyrimidine 
• 24391-39-7 6-bromo-4-chloro-5-cyanopyrrolo[2,3-d]pyrimidin-4-one 
• 1413065-79-8 7-tosyl-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile 

Relevant academic research and scientific papers

Method for selective dehalogenation in pyrimidine fused ring

The invention discloses a method for selective dehalogenation in pyrimidine fused ring. Through heating reaction between zinc powder and acetic acid solution, selective dehalogenation is conducted on pyrimidine ring to maintain original substituents on pyrimidine ring and fused ring. The method comprises few operation steps with high yield, and is applicable to mass production.

Targeting the substrate binding site of E.coli nitrile reductase queF by modeling, substrate and enzyme engineering

Nitrile reductase QueF catalyzes the reduction of 2-amino-5-cyanopyrrolo[2, 3-d]pyrimidin-4-one (preQ0) to 2-amino-5-aminomethylpyrrolo[2,3-d] pyrimidin-4-one (preQ1) in the biosynthetic pathway of the hypermodified nucleoside queuosine. It is the only enzyme known to catalyze a reduction of a nitrile to its corresponding primary amine and could therefore expand the toolbox of biocatalytic reactions of nitriles. To evaluate this new oxidoreductase for application in biocatalytic reactions, investigation of its substrate scope is prerequisite. We report here an investigation of the active site binding properties and the substrate scope of nitrile reductase QueF from Escherichia coli. Screenings with simple nitrile structures revealed high substrate specificity. Consequently, binding interactions of the substrate to the active site were identified based on a new homology model of E.coli QueF and modeled complex structures of the natural and non-natural substrates. Various structural analogues of the natural substrate preQ0 were synthesized and screened with wild-type QueF from E.coli and several active site mutants. Two amino acid residues Cys190 and Asp197 were shown to play an essential role in the catalytic mechanism. Three non-natural substrates were identified and compared to the natural substrate regarding their specific activities by using wild-type and mutant nitrile reductase. Copyright

INHIBITORS OF BRUTON'S TYROSINE KINASE

This application discloses compounds according to generic Formula I: wherein all variables are defined as described herein, which inhibit Btk. The compounds disclosed herein are useful to modulate the activity of Btk and treat diseases associated with excessive Btk activity. The compounds are further useful to treat inflammatory and auto immune diseases associated with aberrant B-cell proliferation such as rheumatoid arthritis. Also disclosed are compositions containing compounds of Formula I and at least one carrier, diluent or excipient.