Jump to main content
Jump to site search

Issue 10, 2010
Previous Article Next Article

Exploring genomes for glycosyltransferases

Author affiliations

Abstract

Glycosyltransferases are one of the largest and most diverse enzyme groups in Nature. They catalyse the synthesis of glycosidic linkages by the transfer of a sugar residue from a donor to an acceptor substrate. These enzymes have been classified into families on the basis of amino acid sequence similarity that are kept updated in the Carbohydrate Active enZyme database (CAZy, http://www.cazy.org/). The repertoire of glycosyltransferases in genomes is believed to determine the diversity of cellular glycan structures, and current estimates suggest that for most genomes about 1% of the coding regions are glycosyltransferases. However, plants tend to have far more glycosyltransferase genes than any other organism sequenced to date, and this can be explained by the highly complex polysaccharide network that form the cell wall and also by the numerous glycosylated secondary metabolites. In recent years, various bioinformatics strategies have been used to search bacterial and plant genomes for new glycosyltransferase genes. These are based on the use of remote homology detection methods that act at the 1D, 2D, and 3D level. The combined use of methods such as profile Hidden Markov Model (HMM) and fold recognition appears to be appropriate for this class of enzyme. Chemometric tools are also particularly well suited for obtaining an overview of multivariate data and revealing hidden latent information when dealing with large and highly complex datasets.

Graphical abstract: Exploring genomes for glycosyltransferases

Back to tab navigation

Publication details

The article was received on 05 Jan 2010, accepted on 07 Apr 2010 and first published on 17 Jun 2010


Article type: Review Article
DOI: 10.1039/C000238K
Citation: Mol. BioSyst., 2010,6, 1773-1781
  •   Request permissions

    Exploring genomes for glycosyltransferases

    S. F. Hansen, E. Bettler, Å. Rinnan, S. B. Engelsen and C. Breton, Mol. BioSyst., 2010, 6, 1773
    DOI: 10.1039/C000238K

Search articles by author

Spotlight

Advertisements