A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana View Full Text


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Article Info

DATE

2001-09

AUTHORS

Bernard Henrissat, Pedro M. Coutinho, Gideon J. Davies

ABSTRACT

The synthesis, modification, and breakdown of carbohydrates is one of the most fundamentally important reactions in nature. The structural and functional diversity of glycosides is mirrored by a vast array of enzymes involved in their synthesis (glycosyltransferases), modification (carbohydrate esterases) and breakdown (glycoside hydrolases and polysaccharide lyases). The importance of these processes is reflected in the dedication of 1–2% of an organism's genes to glycoside hydrolases and glycosyltransferases alone. In plants, these processes are of particular importance for cell-wall synthesis and expansion, starch metabolism, defence against pathogens, symbiosis and signalling. Here we present an analysis of over 730 open reading frames representing the two main classes of carbohydrate-active enzymes, glycoside hydrolases and glycosyltransferases, in the genome of Arabidopsis thaliana. The vast importance of these enzymes in cell-wall formation and degradation is revealed along with the unexpected dominance of pectin degradation in Arabidopsis, with at least 170 open-reading frames dedicated solely to this task. More... »

PAGES

55-72

References to SciGraph publications

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  • 2001-06. A putative plant homolog of the yeast β-1,3-glucan synthase subunit FKS1 from cotton (Gossypium hirsutum L.) fibers in PLANTA
  • 2000-05. Lateral gene transfer and the nature of bacterial innovation in NATURE
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  • 2000-12. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana in NATURE
  • 1994-12. Tracing the spread of fibronectin type III domains in bacterial glycohydrolases in JOURNAL OF MOLECULAR EVOLUTION
  • 2001-09. Integrative approaches to determining Csl function in PLANT MOLECULAR BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1023/a:1010667012056

    DOI

    http://dx.doi.org/10.1023/a:1010667012056

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1038237129

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11554480


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