Journal of South China University of Technology (Natural Science Edition) ›› 2011, Vol. 39 ›› Issue (5): 154-159.doi: 10.3969/j.issn.1000-565X.2011.05.027

• Electronics, Communication & Automation Technology • Previous Articles     Next Articles

Sequence Analysis and Structure Modeling of CYP 725A4

Meng Hai-lin1,2  Wang Jian-feng2,3  Wang Yong2  Zhang Si-liang2  Wang Xiao-ning1   

  1. 1. School of Biological Sciences and Engineering,South China University of Technology,Guangzhou 510006,Guangdong China; 2. Key Laboratory of Synthetic Biology,Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences,Shanghai 200032,China; 3. State Key Laboratory of Bioreactor Engineering,East China University of Science and Technology,Shanghai 200237,China
  • Received:2010-10-14 Revised:2011-02-11 Online:2011-05-25 Published:2011-04-01
  • Contact: 王勇(1974-)，男，博士，教授，主要从事合成生物学研究 E-mail:yongwang@sibs.ac.cn
  • About author:蒙海林(1980-)，男，博士生，主要从事合成生物学研究
  • Supported by:

    国家自然科学基金资助项目(31070030)；上海市“浦江人才计划”项目(09PJ1403600)；上海市“科技创新行动计划”重大科技项目(10dzl910100)；中国科学院知识创新工程重大项目(KSCX2-EW-J-12)

PDF

938

Abstract:

The difficulty in functional expression of CYP725A4 in heterogeneous prokaryotic hosts such as E.coli is a key bottleneck of the heterologous biosynthesis of taxol.In this paper,bioinformatic strategies were employed to analyze the hydrophobic profile and the transmembrane helices of CYP 725A4 sequence,and a molecular phylogenetic tree of CYP 725A4 was constructed.Then,based on the results,the tertiary structures of native and N-terminal truncated CYP 725A4 were reconstructed via the homology modeling,and similar operations were performed for native and truncated versions of cytochrome P450 reductase used for the functional expression of CYP 725A4.PROCHECK results show that the constructed structure models are all reliable.

Key words: bioinformatics, cytochrome P450 hydroxylase, sequence analysis, molecular modeling, functional expression