Aims: In prokaryotes, eukaryotes, and lower plants, N-acetylglutamate (NAG) is the first intermediate in the arginine biosynthetic route. As a model for bond cleavage in living systems, the hydrolysis of amides is very significant in biochemistry and has been studied experimentally and theoretically to study N-acetylglutamate hydrolysis under acidic and basic conditions, using techniques of molecular modelling. Study Design: N-acetylglutamate hydrolysis was studied under acidic and basic conditions to determine variations in chemical properties and favourable conditions, using Mulliken charges and geometric parameters as descriptors, as well as proton affinity, free energy from Gibbs, and constants of equilibrium. Location and duration of the study: between February 2014 and March 2015, Grupo de Investigación Max Planck, Facultad de Química y Farmacia, Universidad del Atlántico. Methodology: Hydrolysis reaction structures under acidic and basic conditions were optimised using molecular mechanics until different molecular descriptors were determined. With the 3-21G and 6-31G* basis sets, the Hartree-Fock (HF) approach was used. Proton affinity, Frontier Molecular Orbitals, Gibbs free energy, and equilibrium constants are some helpful parameters for studying the reactions. Results: In general, reaction profiles showed that the two reactions were favourable; however, a higher favorability for basic hydrolysis was shown in accordance with our preliminary equilibrium constant findings. Conclusion: By analysing the measured Gibbs free energy values, NAG hydrolysis was found to be more favourable under simple conditions. The equilibrium constants measured agree with the hydrolysis favourability under basic conditions, which is compatible with the biochemical process.
Grupo de Investigación Max Planck, Universidad del Atlántico, Km 7 Antigua Vía a Puerto Colombia, Barranquilla, Colombia.
Dr. Sandra Cotes
Departamento de Química y Biología, Universidad del Norte, Km 5 Antigua Vía a Puerto Colombia, Barranquilla, Colombia.
View Book :- https://bp.bookpi.org/index.php/bpi/catalog/book/355