Acta Phys. -Chim. Sin. ›› 2005, Vol. 21 ›› Issue (08): 852-856.doi: 10.3866/PKU.WHXB20050806

• ARTICLE • Previous Articles     Next Articles

Homology Modeling of p-Hydroxymandelate Synthase and Its Molecular Docking with Substrate

LIU Hai-chun; ZOU Jian-wei; ZHANG Bing; ZHUANG Shu-lin; JIANG Yong-jun; YU Qing-sen   

  1. Department of Chemistry, Zhejiang University, Hangzhou 310027; Key Laboratory for Molecular Design and Nutrition Engineering of Ningbo City, Ningbo Institute of Technology, Zhejiang University, Ningbo 315100
  • Received:2004-12-25 Revised:2005-01-24 Published:2005-08-15
  • Contact: ZOU Jian-wei E-mail:jwzou@css.zju.edu.cn

Abstract: p-hydroxymandelate synthase (HMS) and 4-hydroxyphenylpyruvate dioxygenase (HPPD) are highhomology and share the same substrate, p-hydroxyphenylpyruvate(HPP). Using HPPD as a structural template, the 3D structure of HMS was built by homology modeling. Rational analysis of the modeled structure was performed. Subsequently, docking calculations of HPPD and HMS with the substrate HPP were conducted. A comparison of the binding mode of these two enzymes with HPP was made. While the three residues that coordinate to Fe2+, His, His and Glu, are important for the tight binding of both enzymes with the substrate, the conserved residues near the substrate, Leu228, Pro243, Asn245 and Phe364 in HPPD(1T47) and Met187, Thr202 and Ile204 in HMS, play a crucial role in determination of the reaction pathway. This may provide a starting point for the understanding of their difference in catalytic function.

Key words: p-hydroxymandelate synthase, 4-hydroxyphenylpyruvate dioxygenase, Homology modeling, Molecular docking