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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1998-5-28
|
| pubmed:databankReference | |
| pubmed:abstractText |
We report here cloning from the marine gliding bacterium Cytophaga drobachiensis of kappa-carrageenase, a glycoside hydrolase involved in the degradation of kappa-carrageenan. Structural features in the nucleotide sequence are pointed out, including the presence of an octameric omega sequence similar to the ribosome-binding sites of various eukaryotes and prokaryotes. The cgkA gene codes for a protein of 545 aa, with a signal peptide of 35 aa and a 229-aa-long posttranslationaly processed C-terminal domain. The enzyme displays the overall folding and catalytic domain characteristics of family 16 of glycoside hydrolases, which comprises other beta-1,4-alpha-1,3-D/L-galactan hydrolases, beta-1,3-D-glucan hydrolases (laminarinases), beta-1,4-1,3-D-glucan hydrolases (lichenases), and beta-1,4-D-xyloglucan endotransglycosylases. In order to address the origin and evolution of CgkA, a comprehensive phylogenetic tree of family 16 was built using parsimony analysis. Family-16 glycoside hydrolases cluster according to their substrate specificity, regardless of their phylogenetic distribution over eubacteria and eukaryotes. Such a topology suggests that the general homology between laminarinases, agarases, kappa-carrageenases, lichenases, and xyloglucan endotransglycosylases has arisen through gene duplication, likely from an ancestral protein with laminarinase activity.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0737-4038
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
15
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
528-37
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9580981-Amino Acid Sequence,
pubmed-meshheading:9580981-Bacterial Proteins,
pubmed-meshheading:9580981-Base Sequence,
pubmed-meshheading:9580981-Cloning, Molecular,
pubmed-meshheading:9580981-Cytophaga,
pubmed-meshheading:9580981-Evolution, Molecular,
pubmed-meshheading:9580981-Glycoside Hydrolases,
pubmed-meshheading:9580981-Molecular Sequence Data,
pubmed-meshheading:9580981-Phylogeny,
pubmed-meshheading:9580981-Sequence Analysis,
pubmed-meshheading:9580981-Sequence Homology, Amino Acid,
pubmed-meshheading:9580981-Substrate Specificity
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
The kappa-carrageenase of the marine bacterium Cytophaga drobachiensis. Structural and phylogenetic relationships within family-16 glycoside hydrolases.
|
| pubmed:affiliation |
Centre d'Etudes d'Océanologie et de Biologie Marine, CNRS, Roscoff, France.
|
| pubmed:publicationType |
Journal Article
|