Predicting the protein family of Methyl Parathion Hydrolase Online publication date: Sat, 17-May-2008
by Jian Tian, Xuexia Guo, Xiaoyu Chu, Ningfeng Wu, Jun Guo, Bin Yao
International Journal of Bioinformatics Research and Applications (IJBRA), Vol. 4, No. 2, 2008
Abstract: Six motifs of Methyl Parathion Hydrolase (MPH) were discovered using a method based on the Hidden Markov Model (HMM). Most MPH from TrEMBL (Release 48.6) could be recognised by these six motifs. When these six motifs were projected onto the 3D enzyme structure, we discovered that all of them closely surrounded the active centre and might play an important role in structure and function of the enzyme. By comparing the motifs of MPH with PH and analysing the phylogenetic tree, we found that these two enzymes, with substrates differing from only two methyl groups, belonged to two different protein families. The MPH belonged to the Lactamase family, and the PH belonged to the Phosphotriesterase (PTE) family.
Online publication date: Sat, 17-May-2008
If you are not a subscriber and you just want to read the full contents of this article, buy online access here.Complimentary Subscribers, Editors or Members of the Editorial Board of the International Journal of Bioinformatics Research and Applications (IJBRA):
Login with your Inderscience username and password:
Want to subscribe?
A subscription gives you complete access to all articles in the current issue, as well as to all articles in the previous three years (where applicable). See our Orders page to subscribe.
If you still need assistance, please email firstname.lastname@example.org