Research Letters in Biochemistry
Volume 2009 (2009), Article ID 783035, 5 pages
doi:10.1155/2009/783035
Research Letter

What Differs on the Enzymatic Acetylation Mechanisms for Arylamines and Arylhydrazines Substrates? A Theoretical Study

Qing-An Qiao,1 Xiao-Min Sun,2 Jie Jing,1 Xin Chen,1 Hua-Yang Wang,3 Chuan-Lu Yang,3 and Zheng-Ting Cai4

1School of Chemistry and Materials Science, Ludong University, Yantai 264025, China
2Environment Research Institute, Shandong University, Jinan 250100, China
3School of Physics and Electronic Engineering, Ludong University, Yantai 264025, China
4Institute of Theoretical Chemistry, Shandong University, Jinan, Shandong 250100, China

Received 12 May 2009; Accepted 8 July 2009

Academic Editor: George Perry

Copyright © 2009 Qing-An Qiao et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The acetylation mechanisms of several selected typical substrates from experiments, including arylamines and arylhydrazines, are investigated with the density functional theory in this paper. The results indicate that all the transition states are characterized by a four-membered ring structure, and hydralazine (HDZ) is the most potent substrate. The bioactivity for all the compounds is increased in a sequence of PABA≈4-AS<4-MA<5-AS≈INH<HDZ. The conjunction effect and the delocalization of the lone pairs of N atom play a key role in the reaction. All the results are consistent with the experimental data.