| Literature DB >> 19250815 |
Xin Huang1, Yanzhen Yin, Yang Liu, Xiaolong Bai, Zhiming Zhang, Jiayun Xu, Jiacong Shen, Junqiu Liu.
Abstract
Glutathione peroxidase (GPx, EC 1.11.1.9) is a key enzyme involved in scavenging of reactive oxygen species in biological system. For developing an efficient GPx-like antioxidant, catalytically necessary amino acid derivatives which located near the GPx active center were prepared as functional monomers. Via predetermined imprinting with substrate glutathione (GSH), a polymer-based GPx mimic with a similar structure of catalytic center of natural GPx was developed, and it demonstrated high-catalytic efficiency and substrate specificity. The imprinting polymer (I-PEM) exhibits GPx-like activity about three times higher than that of 2-SeCD, a cyclodextrin-based GPx mimic. The detailed studies on kinetics revealed that not only the substrate binding but also positional arrangement of reacting groups contribute significantly to the catalytic efficiency of the peroxidase model.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19250815 DOI: 10.1016/j.bios.2009.01.033
Source DB: PubMed Journal: Biosens Bioelectron ISSN: 0956-5663 Impact factor: 10.618