58026-21-4

Basic information

• Product Name: 2-amino-5-bromo-3-chlorobenzoic acid
• Synonyms: 2-amino-5-bromo-3-chlorobenzoic acid
• CAS NO: 58026-21-4
• Molecular Formula: C₇H₅BrClNO₂
• Molecular Weight: 250.4771
• Mol File: 58026-21-4.mol
• Article Data: 6

Chemical Properties

• Melting Point: 210-211 °C
• Boiling Point: 344.0±42.0 °C(Predicted)
• Appearance: /
• Density: 1.892±0.06 g/cm3(Predicted)
• PKA: 4.18±0.10(Predicted)
• CAS DataBase Reference: 2-amino-5-bromo-3-chlorobenzoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 2-amino-5-bromo-3-chlorobenzoic acid(58026-21-4)
• EPA Substance Registry System: 2-amino-5-bromo-3-chlorobenzoic acid(58026-21-4)

Safety Data

• Hazardous Substances Data: 58026-21-4(Hazardous Substances Data)

Usage

General Description

2-amino-5-bromo-3-chlorobenzoic acid is an organic compound with the molecular formula C7H5BrClNO2. It is a derivative of benzoic acid, with an amino group at the 2-position, a bromine atom at the 5-position, and a chlorine atom at the 3-position. 2-amino-5-bromo-3-chlorobenzoic acid is commonly used in the synthesis of pharmaceuticals and agrochemicals, as well as in organic chemical reactions. It is a white to off-white crystalline powder that is sparingly soluble in water but soluble in organic solvents. Its chemical properties make it useful in various applications, and it is important for researchers and manufacturers in the chemical industry.

Upstream product

• 5794-88-7 5-Bromo-2-aminobenzoic acid 
• 582319-05-9 ethyl 7-chloroindole-3-(3-acetamido-3-carboethoxy)butanoate 
• 1446522-61-7 ethyl 2-acetamido-2-carboethoxy-5-oxo-5-(3-chloro-2-aminophenyl)pentanoate 
• 6388-47-2 2-amino-3-chlorobenzoic acid 

Downstream Products

• 100949-31-3 6-bromo-4,8-dichloro-quinazoline 
• 1227362-25-5 C₁₅H₁₄BrClN₂O₂ 
• 953039-29-7 (2-amino-5-bromo-3-chlorophenyl)methanol 
• 166527-08-8 2-amino-5-bromo-3-chlorobenzaldehyde 
• 1036755-78-8 6-bromo-8-chloroquinazolin-2-ol 

Relevant articles and documents

PROCESS FOR PREPARING A COT INHIBITOR COMPOUND

Disclosed are syntheses of a Cot (cancer Osaka thyroid) inhibitor, which has the formula (I).

KAPPA OPIOID RECEPTOR ANTAGONISTS AND PRODUCTS AND METHODS RELATED THERETO

Compounds are provided that antagonize the kappa-opioid receptor (KOR) and products containing such compounds, as well as to methods of their use and synthesis. Such compounds have the structure of Formula (I), or a pharmaceutically acceptable isomer, racemate, hydrate, solvate, isotope or salt thereof: (I) wherein X, Y, R1, R2, R4, R5 R6, R7, R8 and R11 are as defined herein.

Substituents effects on activity of kynureninase from Homo sapiens and Pseudomonas fluorescens

A series of substituted kynurenines (3-bromo-dl, 3-chloro-dl, 3-fluoro-dl, 3-methyl-dl, 5-bromo-l, 5-chloro-l, 3,5-dibromo-l and 5-bromo-3-chloro-dl) have been synthesized and tested for their substrate activity with human and Pseudomonas fluorescens kynureninase. All of the substituted kynurenines examined have substrate activity with both human as well as P. fluorescens kynureninase. For the human enzyme, 3- and 5-substituted kynurenines have k cat and kcat/Km values higher than l-kynurenine, but less than that of the physiological substrate, 3-hydroxykynurenine. However, 3,5-dibromo- and 5-bromo-3-chlorokynurenine have kcat and kcat/Km values close to that of 3-hydroxykynurenine with human kynureninase. The effects of the 3-halo substituents on the reactivity with human kynureninase may be due to electronic effects and/or halogen bonding. In contrast, for the bacterial enzyme, 3-methyl, 3-halo and 3,5-dihalokynurenines are much poorer substrates, while 3-fluoro, 5-bromo, and 5-chlorokynurenine have kcat and kcat/K m values comparable to that of its physiological substrate, l-kynurenine. Thus, 5-bromo and 5-chloro-l-kynurenine are good substrates for both human as well as bacterial enzyme, indicating that both enzymes have space for substituents in the active site near C-5. The increased activity of the 5-halokynurenines may be due to van der Waals contacts or hydrophobic effects. These results may be useful in the design of potent and/or selective inhibitors of human and bacterial kynureninase.