3679-65-0

Basic information

• Product Name: N-(4-AMINO-PHENYL)-2-HYDROXY-BENZAMIDE
• Synonyms: N1-(4-AMINOPHENYL)-2-HYDROXYBENZAMIDE;N-(4-AMINO-PHENYL)-2-HYDROXY-BENZAMIDE
• CAS NO: 3679-65-0
• Molecular Formula: C₁₃H₁₂N₂O₂
• Molecular Weight: 228.25
• Product Categories: pharmacetical
• Mol File: 3679-65-0.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 356.6°Cat760mmHg
• Flash Point: 169.5°C
• Appearance: /
• Density: 1.35g/cm³
• Vapor Pressure: 1.4E-05mmHg at 25°C
• Refractive Index: 1.722
• CAS DataBase Reference: N-(4-AMINO-PHENYL)-2-HYDROXY-BENZAMIDE(CAS DataBase Reference)
• NIST Chemistry Reference: N-(4-AMINO-PHENYL)-2-HYDROXY-BENZAMIDE(3679-65-0)
• EPA Substance Registry System: N-(4-AMINO-PHENYL)-2-HYDROXY-BENZAMIDE(3679-65-0)

Safety Data

• Hazardous Substances Data: 3679-65-0(Hazardous Substances Data)

Usage

InChI:InChI=1/C13H12N2O2/c14-9-5-7-10(8-6-9)15-13(17)11-3-1-2-4-12(11)16/h1-8,16H,14H2,(H,15,17)

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Relevant articles and documents

Multifunctional bio-based phenol-amine antioxidant, as well as preparation method and application thereof

The invention discloses a multifunctional bio-based phenol-amine antioxidant. The multifunctional bio-based phenol-amine antioxidant includes a compound with a structure shown as a formula in the description, wherein the structural formula of any one of R

Inhibition studies on Mycobacterium tuberculosis N-acetylglucosamine-1- phosphate uridyltransferase (GlmU)

Peptidoglycan is an essential component of the cell wall of bacteria, including Mycobacterium tuberculosis, that provides structural strength and rigidity to enable internal osmotic pressure to be withstood. The first committed step in the biosynthesis of peptidoglycan involves the formation of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) from uridine triphosphate (UTP) and GlcNAc-1-phosphate. This reaction is catalysed by N-acetylglucosamine- 1-phosphate uridyltransferase (GlmU), a bifunctional enzyme with two independent active sites that possess acetyltransferase and uridyltransferase activities. Herein, we report the first inhibition study targeted against the uridyltransferase activity of M. tuberculosis GlmU. A number of potential inhibitors were initially prepared leading to the discovery of active aminoquinazoline-based compounds. The most potent inhibitor in this series exhibited an IC50 of 74 μM against GlmU uridyltransferase activity and serves as a promising starting point for the discovery of more potent inhibitors.