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Bulletin of Botanical Research ›› 2007, Vol. 27 ›› Issue (1): 59-67.doi: 10.7525/j.issn.1673-5102.2007.01.012

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An Analysis of Molecular Structural Character and Function Prediction on 1-deoxy-D-xylulose-5-phosphate Reductoisomerase, a Key Enzyme in Plant Isoprenoid Biosynthesis

LI Rong;WANG Zhe-Zhi   

  1. (College of Life Sciences,Shaanxi Normal University,Xi’an 710062)
  • Received:1900-01-01 Revised:1900-01-01 Online:2007-01-20 Published:2007-01-20
  • Contact: LI Rong
  • Supported by:

Abstract: In the present study, 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Zea mays, Arabidopsis thaliana, Cistus incanus subsp. creticus, Oryza sativa, Artemisia annua and Linum usitatissimum, which were registered in GenBank, were analyzed and predicted by the tools of bioinformatics in the following aspects: the composition of nuclei acid sequences and amino acid sequences, transit peptides, transmembrane topological structure, hydrophobicity or hydrophilicity, secondary and tertiary structure of protein, molecular phylogenetic evolution and so on. The results as following: the full-length gene of DXR contains an opening reading frame, 5′-untranstrated region and 3′-untranstrated region; DXR is a hydrophilic and non-transmembrane protein with transit peptides; the amino acid sequences of DXR include two functional DXR binding motifs and two functional NADPH binding motifs; the main motif of predicted secondary structure of DXR are alpha helix and random coil, beta turn and extended strand are spreaded in the whole secondary structure of protein; the predicted tertiary structure of functional domain of DXR consists of three domains arranged to form an overall V-shaped molecule. The N-terminal domain forms one arm of the V and C-terminal domain forms the second arm of the V. The apical region of the V is formed by a connective N-terminal and C-terminal domain.

Key words: plant isoprenoid biosynthesis, 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR), molecular structure, function prediction, bioinformatics

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