Linked Life Data

16697989

Source:http://linkedlifedata.com/resource/pubmed/id/16697989

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2006-6-19
pubmed:abstractText
We previously reported the isolation and cDNA cloning of an endolytic alginate lyase, HdAly, from abalone Haliotis discus hannai [Carbohydr. Res.2003, 338, 2841-2852]. Although HdAly preferentially degraded mannuronate-rich substrates, it was incapable of degrading unsaturated oligomannuronates smaller than tetrasaccharide. In the present study, we used conventional chromatographic techniques to isolate a novel unsaturated-trisaccharide-degrading enzyme, named HdAlex, from the digestive fluid of the abalone. The HdAlex showed a molecular weight of 32,000 on SDS-PAGE and could degrade not only unsaturated trisaccharide but also alginate and mannuronate-rich polymers at an optimal pH and temperature of 7.1 and 42 degrees C, respectively. Upon digestion of alginate polymer, HdAlex decreased the viscosity of the alginate at a slower rate than did HdAly, producing only unsaturated disaccharide without any intermediate oligosaccharides. These results indicate that HdAlex degrades the alginate polymer in an exolytic manner. Because HdAlex split saturated trisaccharide producing unsaturated disaccharide, we considered that this enzyme cleaved the alginate at the second glycoside linkage from the reducing terminus. The primary structure of HdAlex was deduced with cDNAs amplified from an abalone hepatopancreas cDNA library by the polymerase chain reaction. The translational region of 822 bp in the total 887-bp sequence of HdAlex cDNA encoded an amino-acid sequence of 273 residues. The N-terminal sequence of 16 residues, excluding the initiation methionine, was regarded as the signal peptide of this enzyme. The amino-acid sequence of the remaining 256 residues shared 62-67% identities with those of the polysaccharide lyase family-14 (PL14) enzymes such as HdAly and turban-shell alginate lyase SP2. To our knowledge, HdAlex is the first exolytic oligoalginate lyase belonging to PL14.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0008-6215
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
341
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1809-19
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16697989-Alginates, pubmed-meshheading:16697989-Amino Acid Sequence, pubmed-meshheading:16697989-Animals, pubmed-meshheading:16697989-Binding Sites, pubmed-meshheading:16697989-Carbohydrate Sequence, pubmed-meshheading:16697989-Chromatography, Thin Layer, pubmed-meshheading:16697989-Cloning, Molecular, pubmed-meshheading:16697989-DNA, Complementary, pubmed-meshheading:16697989-Disaccharides, pubmed-meshheading:16697989-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16697989-Hexuronic Acids, pubmed-meshheading:16697989-Hydrogen-Ion Concentration, pubmed-meshheading:16697989-Molecular Sequence Data, pubmed-meshheading:16697989-Mollusca, pubmed-meshheading:16697989-Oligosaccharides, pubmed-meshheading:16697989-Polysaccharide-Lyases, pubmed-meshheading:16697989-Recombinant Proteins, pubmed-meshheading:16697989-Sequence Alignment, pubmed-meshheading:16697989-Sequence Analysis, DNA, pubmed-meshheading:16697989-Sequence Homology, Amino Acid, pubmed-meshheading:16697989-Substrate Specificity
pubmed:year
2006
pubmed:articleTitle
A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner.
pubmed:affiliation
Laboratory of Marine Biotechnology and Microbiology, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't