| http://purl.uniprot.org/citations/17269933 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17269933 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17269933 | http://www.w3.org/2000/01/rdf-schema#comment | "Carrageenans are sulfated galactans found in the cell walls of red seaweeds. They are classified according to the number and the position of sulfate ester groups. lambda-Carrageenan is the most sulfated carrageenan and carries at least three sulfates per disaccharide unit. The sole known depolymerizing enzyme of lambda-carrageenan, the lambda-carrageenase from Pseudoalteromonas carrageenovora, has been purified, cloned and sequenced. Sequence analyses have revealed that the lambda-carrageenase, referred to as CglA, is the first member of a new family of GHs (glycoside hydrolases), which is unrelated to families GH16, that contains kappa-carrageenases, and GH82, that contains iota-carrageenases. This large enzyme (105 kDa) features a low-complexity region, suggesting the presence of a linker connecting at least two independent modules. The N-terminal region is predicted to fold as a beta-propeller. The main degradation products have been purified and characterized as neo-lambda-carratetraose [DP (degree of polymerization) 4] and neo-lambda-carrahexaose (DP6), indicating that CglA hydrolyses the beta-(1-->4) linkage of lambda-carrageenan. LC-MALLS (liquid chromatography-multi-angle laser light scattering) and (1)H-NMR monitoring of the enzymatic degradation of lambda-carrageenan indicate that CglA proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration. Using 2-aminoacridone-labelled neo-lambda-carrabiose oligosaccharides, in the present study we demonstrate that the active site of CglA comprises at least 8 subsites (-4 to +4) and that a DP6 oligosaccharide binds in the subsites -4 to +2 and can be hydrolysed into DP4 and DP2."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20061359"xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20061359"xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Barbeyron T."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Barbeyron T."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Kloareg B."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Kloareg B."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Michel G."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Michel G."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Helbert W."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Helbert W."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Genicot S."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Genicot S."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Colin S."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Colin S."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Guibet M."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/author | "Guibet M."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/pages | "105-114"xsd:string |
| http://purl.uniprot.org/citations/17269933 | http://purl.uniprot.org/core/pages | "105-114"xsd:string |