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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2009-1-12
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pubmed:abstractText |
Bacteria in a biofilm are enmeshed in a self-synthesized extracellular polysaccharide matrix (PGA), which is a linear polymer of beta(1,6)-linked N-acetylglucosamine (GlcNAc) residues. Dispersin B (DspB), a soluble glycoside hydrolase produced by the periodontal pathogen Actinobacillus actinomycetemcomitans degrades PGA. The enzyme DspB is an alpha/beta TIM-barrel protein and belongs to family 20 glycosyl hydrolases members. The enzyme activity of DspB with regard to its substrate specificity towards beta(1,6)-linked GlcNAc polymers and its endo/exo character was investigated through ligand docking and the hydrolysis of synthetic oligosaccharides. Ligand docking analysis suggested that beta(1,6)-linked GlcNAc oligosaccharide bound to the active site better that beta(1,4)-linked GlcNAc oligosaccharide. Our combined results indicate that DspB is an exo-acting enzyme that hydrolyzes beta(1,6)-linked N-acetylglucosamine oligomers.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0236-5383
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
439-51
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pubmed:meshHeading |
pubmed-meshheading:19133500-Actinobacillus actinomycetemcomitans,
pubmed-meshheading:19133500-Amino Acid Sequence,
pubmed-meshheading:19133500-Bacterial Proteins,
pubmed-meshheading:19133500-Biofilms,
pubmed-meshheading:19133500-Carbohydrate Sequence,
pubmed-meshheading:19133500-Catalytic Domain,
pubmed-meshheading:19133500-Escherichia coli,
pubmed-meshheading:19133500-Glycoside Hydrolases,
pubmed-meshheading:19133500-Hydrolysis,
pubmed-meshheading:19133500-Ligands,
pubmed-meshheading:19133500-Models, Molecular,
pubmed-meshheading:19133500-Molecular Sequence Data,
pubmed-meshheading:19133500-Oligosaccharides,
pubmed-meshheading:19133500-Polysaccharides, Bacterial,
pubmed-meshheading:19133500-Sequence Homology, Amino Acid,
pubmed-meshheading:19133500-Substrate Specificity,
pubmed-meshheading:19133500-Thermodynamics
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pubmed:year |
2008
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pubmed:articleTitle |
Modeling and biochemical analysis of the activity of antibiofilm agent Dispersin B.
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pubmed:affiliation |
Academic Systems and Technologies, University of Medicine and Dentistry of New Jersey, Newark, NJ 07103, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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