• DocumentCode
    2678465
  • Title

    Automatic Prediction of Enzyme Functions from Domain Compositions Using Enzyme Reaction Prediction Scheme

  • Author

    Huang, Chuan-Ching ; Lin, Chun-Yuan ; Chang, Cheng-Wen ; Tang, Chuan Yi

  • Author_Institution
    Dept. of Comput. Sci., NTHU, Hsinchu, Taiwan
  • fYear
    2012
  • fDate
    28-30 May 2012
  • Firstpage
    82
  • Lastpage
    85
  • Abstract
    Proteins perform most important biochemical reactions in organisms, such as the catalysis, signal transduction, and transport of nutrients. The urgent need of automatic annotation is due to the advent of high-throughput sequencing techniques in the post-genomic era. Proteins consist of domains which are elementary building units of protein folding, function, and evolution. The evidence of protein function is convincible to deduce from its domain composition. For enzyme function prediction, efficiency and reliability become more and more important in the recent researches. This study proposed an enzyme reaction prediction scheme with a learning model for enzyme function predictions to avoid the exponential enumeration problem of frequent item-sets in the association rule algorithm. Our work also contributed to the prediction of multiple reactions due to the nature of enzymes.
  • Keywords
    biology; enzymes; association rule algorithm; automatic annotation; automatic prediction; biochemical reactions; domain compositions; elementary building units; enzyme functions; enzyme reaction prediction scheme; exponential enumeration problem; nutrient transport; post genomic era; signal transduction; Association rules; Bioinformatics; Databases; Prediction algorithms; Proteins; association rule algorithm; domain compositions; enzyme reaction prediction; k-fold cross-validation;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Biomedical Engineering and Biotechnology (iCBEB), 2012 International Conference on
  • Conference_Location
    Macau, Macao
  • Print_ISBN
    978-1-4577-1987-5
  • Type

    conf

  • DOI
    10.1109/iCBEB.2012.88
  • Filename
    6245062