Document of bibliographic reference 67411

BibliographicReference record

Type

Bibliographic resource

Type of document

Journal article

BibLvlCode

AS

Title

The sulphated-galactan hydrolases, agarases and carrageenases: structural biology and molecular evolution

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.

WebOfScience code

https://www.webofscience.com/wos/woscc/full-record/WOS:000168120500016

Bibliographic citation

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

Topic

Marine

Is peer reviewed

true

Access rights

open access

Is accessible for free

true