IMIS | Flanders Marine Institute
 

Flanders Marine Institute

Platform for marine research

IMIS

Publications | Institutes | Persons | Datasets | Projects | Maps
[ report an error in this record ]basket (0): add | show Printer-friendly version

The sulphated-galactan hydrolases, agarases and carrageenases: structural biology and molecular evolution
Barbeyron, T.; Flament, D.; Michel, G.; Potin, Ph.; Kloareg, B. (2001). The sulphated-galactan hydrolases, agarases and carrageenases: structural biology and molecular evolution. Cah. Biol. Mar. 42(1-2): 169-183
In: Cahiers de Biologie Marine. Station Biologique de Roscoff: Paris. ISSN 0007-9723, more
Peer reviewed article  

Also published as
  • Barbeyron, T.; Flament, D.; Michel, G.; Potin, Ph.; Kloareg, B. (2001). The sulphated-galactan hydrolases, agarases and carrageenases: structural biology and molecular evolution, in: Proceedings of the International Workshop "Current approaches in basic and applied phycology". Cahiers de Biologie Marine, 42(1-2): pp. 169-183, more

Available in Authors 

Keyword
    Marine

Authors  Top 
  • Barbeyron, T.
  • Flament, D.
  • Michel, G.

Abstract
    The carrageenans and agars are major cell-wall polysaccharides from red algae. These sulphated galactans are degraded by enzymes, called carrageenases and agarases that display strict substrate specifities and recognize the pattern of galactan sulphation. From a set of various marine bacteria enzymes, we have investigated the influence of ester-sulphate groups, of D/L isomery and of linkage anomery on the structure-function relationships of the specific galactan hydrolases that degrade sulphated polysaccharides. With this aim, we have cloned a representative set of sulphated-galactan hydrolase genes. The sequence analysis methods indicate that the beta-agarases and kappa- carrageenases display secondary structure similarities with members of family 16 of glycoside hydrolases. In contrast, the L-carrageenases have no structural relationships with the family-16 beta-agarases and kappa-carrageenases and they constitute a novel structural family of glycan hydrolases. As a preliminary step towards the functional analysis of these two structural families, we have overexpressed the L- and kappa-carrageenase genes in Escherichia coli and crystals from these enzymes have been obtained. Finally, an alpha-agarase, the only one galactanase known to cleave the alpha-1,3 linkage in agarose has no similarity with other glycoside hydrolases or proteins and display some interesting characteristics. To date, this enzyme is an unclassified glycoside hydrolase.

All data in IMIS is subject to the VLIZ privacy policy Top | Authors