4-Nitrophenyl Hexanoate (CAS 956-75-2)
QUICK LINKS
4-Nitrophenyl hexanoate is a compound of interest in organic chemistry and enzymology due to its ability to act as a substrate for esterases and lipases, enzymes that hydrolyze ester bonds. In enzyme kinetics studies, this ester is frequently used to assess the activity and specificity of these enzymes, providing insights into their mechanisms of action. This has implications for understanding lipid metabolism and the synthesis of biodiesel, where such enzymes are employed to catalyze the transesterification of triglycerides. In organic synthesis, 4-nitrophenyl hexanoate can be employed in the synthesis of complex organic molecules, serving as an esterification agent that introduces hexanoate groups. Additionally, the nitrophenyl moiety of the molecule is known to release a colored product upon enzymatic cleavage, which is useful in spectrophotometric assays that measure enzyme activity and kinetic parameters.
4-Nitrophenyl Hexanoate (CAS 956-75-2) References
- Reactions within association complexes: the reaction of imidazole with substituted phenyl acetates in the presence of detergents in aqueous solution. | Pirinccioglu, N., et al. 2000. J Org Chem. 65: 2537-43. PMID: 10789468
- A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis. | De Simone, G., et al. 2004. J Biol Chem. 279: 6815-23. PMID: 14617621
- Catalysis by hydrophobically modified poly(propylenimine) dendrimers having quaternary ammonium and tertiary amine functionality. | Murugan, E., et al. 2004. Langmuir. 20: 8307-12. PMID: 15350107
- Bile-salt-stimulated lipase and mucins from milk of 'secretor' mothers inhibit the binding of Norwalk virus capsids to their carbohydrate ligands. | Ruvoën-Clouet, N., et al. 2006. Biochem J. 393: 627-34. PMID: 16266293
- Expression and characterization of a novel enantioselective lipase from Aspergillus fumigatus. | Shangguan, JJ., et al. 2012. Appl Biochem Biotechnol. 168: 1820-33. PMID: 23054817
- Experimental and theoretical study of the mechanism of hydrolysis of substituted phenyl hexanoates catalysed by globin in the presence of surfactant. | Ercan, S., et al. 2014. J Mol Model. 20: 2096. PMID: 24562853
- Purification and characterization of esterase 2B of the house mouse, Mus musculus. | Lexow, U., et al. 1980. Eur J Biochem. 107: 123-30. PMID: 6772441
- Purification and characterization of esterase 1F, the albumin esterase of the house mouse (Mus musculus). | Otto, J., et al. 1981. Eur J Biochem. 116: 285-91. PMID: 6788549
- Purification and characterization of esterase 6A, a trimeric esterase of the house mouse (Mus musculus). | Oehm, HC., et al. 1982. Eur J Biochem. 129: 157-63. PMID: 7160378
- Association of bile-salt-dependent lipase with membranes of human pancreatic microsomes. | Bruneau, N., et al. 1995. Eur J Biochem. 233: 209-18. PMID: 7588748
- An investigation of activities and paraoxon sensitivities of hepatic aliesterases in beta-naphthoflavone-treated rats. | Watson, AM., et al. 1994. Toxicol Lett. 71: 217-25. PMID: 8160210
- Esterase-30 (ES-30) of the house mouse: biochemical characterization and genetics of a new carboxylesterase isozyme linked to cluster-2 loci on chromosome 8. | Ronai, A., et al. 1993. Biochem Genet. 31: 279-94. PMID: 8274135
- Investigation of two glycosylated forms of bile-salt-dependent lipase in human pancreatic juice. | Mas, E., et al. 1997. Eur J Biochem. 243: 299-305. PMID: 9030752
- Association of bile-salt-dependent lipase with membranes of human pancreatic microsomes is under the control of ATP and phosphorylation. | Pasqualini, E., et al. 1997. Biochem J. 327 (Pt 2): 527-35. PMID: 9359426
- Pancreatic bile salt-dependent lipase activity in serum of normolipidemic patients. | Caillol, N., et al. 1997. Lipids. 32: 1147-53. PMID: 9397399
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
4-Nitrophenyl Hexanoate, 1 g | sc-486520 | 1 g | $159.00 |