124738-81-4

Basic information

• Product Name: 2-Amino-4-chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
• Synonyms: 2-Amino-4-chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
• CAS NO: 124738-81-4
• Molecular Formula: C₇H₄ClN₅
• Molecular Weight: 193.59316
• Mol File: 124738-81-4.mol

Chemical Properties

• Melting Point: >300 °C
• Boiling Point: 286.9±50.0 °C(Predicted)
• Appearance: /
• Density: 1.83±0.1 g/cm3(Predicted)
• PKA: 8.10±0.20(Predicted)
• CAS DataBase Reference: 2-Amino-4-chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Amino-4-chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile(124738-81-4)
• EPA Substance Registry System: 2-Amino-4-chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile(124738-81-4)

Safety Data

• Hazardous Substances Data: 124738-81-4(Hazardous Substances Data)

Usage

General Description

2-Amino-4-chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile is a chemical compound with the molecular formula C7H4ClN5. It is an organic compound that contains a pyrrolopyrimidine ring with an amino group and a chloro group attached to it. Additionally, it contains a carbonitrile group, which is a nitrile group attached to a carbon atom. 2-Amino-4-chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile is used in the synthesis of various pharmaceuticals and agrochemicals, due to its unique structure and reactivity. It has also been studied for its potential medicinal properties, particularly in the treatment of cancer and other diseases.

Upstream product

• 124738-80-3 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carboxamide 
• 69205-79-4 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile 
• 124738-76-7 methyl 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carboxylate 
• 124738-78-9 methyl 2-amino-7-(N-t-butoxycarbonyl)pyrrolo<2,3-d>pyrimidin-4-one-5-carboxylate 

Downstream Products

• 124738-82-5 C₂₈H₂₄ClN₅O₅ 

Relevant articles and documents

Nitrile reductase from Geobacillus kaustophilus: A potential catalyst for a new nitrile biotransformation reaction

The cloning, expression and characterization of a nitrile reductase (NRed) from the thermophile Geobacillus kaustophilus is reported. The enzyme shows a 12-fold increase in activity in response to a temperature change from 25 °C to 65 °C. The substrate scope regarding its biocatalytic applicability was investigated by testing a range of common nitriles. The narrow substrate range observed for the wild-type enzyme prompted the rational design of GkNRed active site mutants based on a previously published homology model from Bacillus subtilis. The activities of the mutants and the wild-type enzyme were investigated in their structure-function relationship regarding the natural substrate 7-cyano-7-deazaguanine (preQ0) as well as a range of synthesized preQ0-like substrate structures. A distinct dependence of the wild-type enzyme activity on specific structural modifications of the natural substrate was observed. Two non-natural nitriles derived from preQ 0 could be reduced to their corresponding amino compounds. Copyright

Inhibitory Kappa B Kinase α (IKKα) Inhibitors That Recapitulate Their Selectivity in Cells against Isoform-Related Biomarkers

IKKβ plays a central role in the canonical NF-kB pathway, which has been extensively characterized. The role of IKKα in the noncanonical NF-kB pathway, and indeed in the canonical pathway as a complex with IKKβ, is less well understood. One major reason for this is the absence of chemical tools designed as selective inhibitors for IKKα over IKKβ. Herein, we report for the first time a series of novel, potent, and selective inhibitors of IKKα. We demonstrate effective target engagement and selectivity with IKKα in U2OS cells through inhibition of IKKα-driven p100 phosphorylation in the noncanonical NF-kB pathway without affecting IKKβ-dependent IKappa-Bα loss in the canonical pathway. These compounds represent the first chemical tools that can be used to further characterize the role of IKKα in cellular signaling, to dissect this from IKKβ and to validate it in its own right as a target in inflammatory diseases.

The synthesis of 7-deazaguanines as potential inhibitors of guanosine triphosphate cyclohydrolase I

Variously substituted 7-deazaguanines are of interest as inhibitors of GTP cyclohydrolase I, the first enzyme in the biosynthetic pathway leading to dihydrofolate and tetrahydrobiopterin. Methods are described for the synthesis of 7-deazaguanines substituted at positions 2, 6 and 9 (purine numbering) such that a wide diversity of compounds can be prepared. These methods supplement our previous work that established routes for the synthesis of 7- and 8-substituted 7-deazaguanines. Emphasis is placed on the properties of 2-thioalkyl pyrimidines as intermediates because they provide the basis for a traceless solid-state synthesis of purines, pteridines, and their analogues. Compounds prepared have been assessed in a primary screen for their ability to inhibit GTPCH I and 8-methyldeazaguanine has been shown to be significantly more potent than any inhibitor yet described. Several compounds appeared to undergo transformation by GTPCH I; with the aid of a model reaction, their behaviour can be interpreted in the context of the mechanism of the hydrolytic phase of GTPCH I.