Proceedings of the Korean Society for Bioinformatics Conference (한국생물정보학회:학술대회논문집)

Korean Society for Bioinformatics (한국생명정보학회)
권호 표지

Probing Starch Biosynthesis Enzyme Isoforms by Visualization of Conserved Secondary Structure Patterns

  • Vorapreeda, Tayvich (Biochemical Engineering and Pilot Plant Research and Development Unit. National Center for Genetic Engineering and Biotechnology & King Mongkut's University of Technology Thonburi) ;
  • Kittichotirat, Weerayuth (Bioinformatics Program, King Mongkut's University of Technology Thonburi) ;
  • Meechai, Asawin (epartment of Chemical Engineering, King Mongkut's University of Technology Thonburi) ;
  • Bhumiratana, Sakarindr (Biochemical Engineering and Pilot Plant Research and Development Unit. National Center for Genetic Engineering and Biotechnology & King Mongkut's University of Technology Thonburi, Department of Chemical Engineering, King Mongkut's University of Technology Thonburi, Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi) ;
  • Cheevadhanarak, Supapon (Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi)
  • Published : 2005.09.22
Download PDF
⟨ Previous Next ⟩

Abstract

Generally, enzymes in the starch biosynthesis pathway exist in many isoforms, contributing to the difficulties in the dissection of their specific roles in controlling starch properties. In this study, we present an algorithm as an alternative method to classify isoforms of starch biosynthesis enzymes based on their conserved secondary structures. Analysis of the predicted secondary structure of plant soluble starch synthase I (SSI) and soluble starch synthase II (SSII) demonstrates that these two classes of isoform can be reclassified into three subsets, SS-A, SS-B and SS-C, according to the differences in the secondary structure of the protein at C-terminus. SS-A reveals unique structural features that are conserved only in cereal plants, while those of SS-B are found in all plants and SS-C is restricted to barley. These findings enable us to increase the accuracy in the estimation of evolutionary distance between isoforms of starch synthases. Moreover, it facilitates the elucidation of correlations between the functions of each enzyme isoforms and the properties of starches. Our secondary structure analysis tool can be applicable to study the functions of other plant enzyme isoforms of economical importance.

Keywords