3-Aminobenzamide
Names | |
---|---|
Preferred IUPAC name
3-Aminobenzamide | |
Other names
| |
Identifiers | |
3544-24-9 | |
3D model (Jmol) | Interactive image |
ChEBI | CHEBI:64042 |
ChemSpider | 1583 |
ECHA InfoCard | 100.020.534 |
EC Number | 222-586-9 |
PubChem | 1645 |
| |
| |
Properties | |
C7H8N2O | |
Molar mass | 136.15 g·mol−1 |
Appearance | Off-white powder |
Density | 1.233g/cm3 |
Melting point | 115 to 116 °C (239 to 241 °F; 388 to 389 K) |
Boiling point | 329 °C (624 °F; 602 K) |
log P | 0.33 |
Hazards | |
Safety data sheet | Sigma-Aldrich |
GHS pictograms | |
GHS signal word | DANGER |
H302, H315, H319, H335 | |
P351, P338 | |
EU classification (DSD) |
Xi |
R-phrases | R36/37/38 |
S-phrases | S26-36 |
NFPA 704 | |
Lethal dose or concentration (LD, LC): | |
LD50 (median dose) |
1000mg/kg (oral, bird) |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
Infobox references | |
3-Aminobenzamide is a benzamide. It is an off-white powder and has the chemical formula C7H8N2O.
Preparation
3-Aminobenzamide can be prepared though the reduction of 3-nitrobenzamide by catalytic hydrogenation.[1]
Uses
3-Aminobenzamide is an inhibitor of poly ADP ribose polymerase (PARP), an enzyme responsible for DNA repair, transcription control, and programmed cell death.<ref="Purnell1980"/> When PARP is activated it rapidly uses up stores of nicotinamide adenine dinucleotide (NAD+) in the cell as it performs DNA repair. Low levels of NAD+ deplete the amount of ATP found in the cell which can lead to cell death.[2] The structure of 3-aminobenzamide is similar to that of NAD+ so it binds to PARP and prevents it from using up NAD+. PARP is often a target of cancer therapy and so 3-aminobenzamide could potentially be used as an anticancer drug.[3]
References
- ↑ Purnell, M. R; Whish, W. J. D. (1980). "Novel inhibitors of poly(ADP-ribose) synthetase". Biochem. J. 185 (3): 775–777. doi:10.1042/bj1850775. PMC 1161458. PMID 6248035.
- ↑ 3-Aminobenzamide Product Information, Sigma-Aldrich, Accessed October 19, 2012
- ↑ Karlberg, T.; Hammarström, M.; Schütz, P.; Scensson, L.; Schüler, H. (2010). "Crystal Structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888". Biochemistry. 49 (6): 1056–1058. doi:10.1021/bi902079y. PMID 20092359.