Title: Predicting the protein family of Methyl Parathion Hydrolase

Authors: Jian Tian, Xuexia Guo, Xiaoyu Chu, Ningfeng Wu, Jun Guo, Bin Yao

Addresses: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. ' Agricultural By-Products Processing Research Institute, Academy of Planning and Designing of the Ministry of Agriculture, Beijing 100026, China. ' Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. ' Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. ' Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. ' Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China

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.

Keywords: methyl parathion hydrolase; MPH; hidden Markov models; HMM; bioinformatics; motifs; phylogenetic tree; enzyme structure; protein families.

DOI: 10.1504/IJBRA.2008.018346

International Journal of Bioinformatics Research and Applications, 2008 Vol.4 No.2, pp.201 - 210

Available online: 17 May 2008 *

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