185256-47-7

Basic information

• Product Name: tert-Butyl (2-phenylcyclopropyl)carbamate
• Synonyms: tert-Butyl (2-phenylcyclopropyl)carbamate;(1R-trans)-(2-Phenylcyclopropyl)carbamic acid 1,1-dimethylethyl ester;trans-tert-butyl ((1R,2S)-2-phenylcyclopropyl)carbamate(WXG00866)
• CAS NO: 185256-47-7
• Molecular Formula: C₁₄H₁₉NO₂
• Molecular Weight: 233.30616
• Mol File: 185256-47-7.mol
• Article Data: 6

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: tert-Butyl (2-phenylcyclopropyl)carbamate(CAS DataBase Reference)
• NIST Chemistry Reference: tert-Butyl (2-phenylcyclopropyl)carbamate(185256-47-7)
• EPA Substance Registry System: tert-Butyl (2-phenylcyclopropyl)carbamate(185256-47-7)

Safety Data

• Hazardous Substances Data: 185256-47-7(Hazardous Substances Data)

Usage

General Description

Tert-butyl (2-phenylcyclopropyl)carbamate is a chemical compound that is used as a carbamate insecticide. tert-Butyl (2-phenylcyclopropyl)carbamate is an organic compound with the formula C13H19NO2 and is structurally related to the widely used insecticide carbaryl. It is a white crystalline solid that is commonly used in agricultural and household products for pest control. Tert-butyl (2-phenylcyclopropyl)carbamate works by inhibiting the activity of the enzyme acetylcholinesterase in insects, leading to paralysis and ultimately death. However, it is important to note that this compound should be handled with caution as it may be toxic to humans and animals if ingested or inhaled in large quantities.

Upstream product

• 3471-10-1 (1R,2R)-trans-2-phenyl-1-cyclopropanecarboxylic acid 
• 75-65-0 tert-butyl alcohol 
• 24424-99-5 di-tert-butyl dicarbonate 
• 95-62-5 (1R,2S)-1-amino-2-phenylcyclopropane 
• 5685-38-1 2-phenyl-cyclopropanecarboxylic acid 
• 928054-80-2 (-)-trans-2-phenylcyclopropanecarboxylic acid (2-hydroxy-1-phenylethyl)amide 
• 4192-77-2 ethyl cinnamate 
• 946-38-3 ethyl 2-phenylcyclopropylcarboxylate 
• 110659-58-0 (1R,2R)-1-hydroxymethyl-2-phenylcyclopropane 
• 4407-36-7 (2E)-3-phenyl-2-propen-1-ol 
• 847644-86-4 ((1SR,2RS)-tert-butyl-2-phenylcyclopropyl)carbamate 
• 946-39-4 ethyl rac-(1S,2S)-2-phenylcycloproanecarboxylate 
• 97-71-2 (1R,2R)-2-phenyl-cyclopropanecarboxylic acid ethyl ester 
• 97-71-2 ethyl (S,S)-2-phenylcyclopropane-1-carboxylate 

Downstream Products

• 95-62-5 (1R,2S)-1-amino-2-phenylcyclopropane 
• 3721-28-6 (1S,2R)-tranylcypromine 
• 1986-47-6 tranylcypromine hydrochloride 

Relevant articles and documents

A catalytic enantioselective synthesis of antidepressant tranylcypromine

An efficient catalytic enantioselective synthesis of the antidepressant tranylcypromine is described.

KDM1A INHIBITORS FOR THE TREATMENT OF DISEASE

Disclosed herein are new compounds and compositions and their application as pharmaceuticals for the treatment of diseases. Methods of inhibition of KDMIA, and methods of increasing gamma globin gene expression in a human or animal subject are also provided for the treatment diseases such as sickle cell disease.

Biochemical, structural, and biological evaluation of tranylcypromine derivatives as inhibitors of histone demethylases LSD1 and LSD2

LSD1 and LSD2 histone demethylases are implicated in a number of physiological and pathological processes, ranging from tumorigenesis to herpes virus infection. A comprehensive structural, biochemical, and cellular study is presented here to probe the potential of these enzymes for epigenetic therapies. This approach employs tranylcypromine as a chemical scaffold for the design of novel demethylase inhibitors. This drug is a clinically validated antidepressant known to target monoamine oxidases A and B. These two flavoenzymes are structurally related to LSD1 and LSD2. Mechanistic and crystallographic studies of tranylcypromine inhibition reveal a lack of selectivity and differing covalent modifications of the FAD cofactor depending on the enantiomeric form. These findings are pharmacologically relevant, since tranylcypromine is currently administered as a racemic mixture. A large set of tranylcypromine analogues were synthesized and screened for inhibitory activities. We found that the common evolutionary origin of LSD and MAO enzymes, despite their unrelated functions and substrate specificities, is reflected in related ligand-binding properties. A few compounds with partial enzyme selectivity were identified. The biological activity of one of these new inhibitors was evaluated with a cellular model of acute promyelocytic leukemia chosen since its pathogenesis includes aberrant activities of several chromatin modifiers. Marked effects on cell differentiation and an unprecedented synergistic activity with antileukemia drugs were observed. These data demonstrate that these LSD1/2 inhibitors are of potential relevance for the treatment of promyelocytic leukemia and, more generally, as tools to alter chromatin state with promise of a block of tumor progression.