Source:http://linkedlifedata.com/resource/pubmed/id/15639245
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-1-10
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pubmed:abstractText |
Alternansucrase (EC 2.4.1.140) is a d-glucansucrase that synthesizes an alternating alpha-(1-->3), (1-->6)-linked d-glucan from sucrose. It also synthesizes oligosaccharides via d-glucopyranosyl transfer to various acceptor sugars. Two of the more efficient monosaccharide acceptors are D-tagatose and L-glucose. In the presence of d-tagatose, alternansucrase produced the disaccharide alpha-d-glucopyranosyl-(1-->1)-beta-D-tagatopyranose via glucosyl transfer. This disaccharide is analogous to trehalulose. We were unable to isolate a disaccharide product from L-glucose, but the trisaccharide alpha-D-glucopyranosyl-(1-->6)-alpha-d-glucopyranosyl-(1-->4)-l-glucose was isolated and identified. This is analogous to panose, one of the structural units of pullulan, in which the reducing-end D-glucose residue has been replaced by its L-enantiomer. The putative L-glucose disaccharide product, produced by glucoamylase hydrolysis of the trisaccharide, was found to be an acceptor for alternansucrase. The disaccharide, alpha-D-glucopyranosyl-(1-->4)-L-glucose, was a better acceptor than maltose, previously the best known acceptor for alternansucrase. A structure comparison of alpha-D-glucopyranosyl-(1-->4)-L-glucose and maltose was performed through computer modeling to identify common features, which may be important in acceptor affinity by alternansucrase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Hexoses,
http://linkedlifedata.com/resource/pubmed/chemical/alternansucrase,
http://linkedlifedata.com/resource/pubmed/chemical/tagatose
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0008-6215
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
340
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
257-62
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15639245-Binding Sites,
pubmed-meshheading:15639245-Carbohydrate Sequence,
pubmed-meshheading:15639245-Disaccharides,
pubmed-meshheading:15639245-Glucose,
pubmed-meshheading:15639245-Glycosyltransferases,
pubmed-meshheading:15639245-Hexoses,
pubmed-meshheading:15639245-Molecular Sequence Data,
pubmed-meshheading:15639245-Molecular Structure,
pubmed-meshheading:15639245-Stereoisomerism,
pubmed-meshheading:15639245-Structure-Activity Relationship,
pubmed-meshheading:15639245-Thermodynamics
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pubmed:year |
2005
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pubmed:articleTitle |
Alternansucrase acceptor reactions with D-tagatose and L-glucose.
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pubmed:affiliation |
Bioproducts and Biocatalysis Research Unit, National Center for Agricultural Utilization Research, Agricultural Research Service, United States Department of Agriculture, 1815 North University Street, Peoria, IL 61604, USA. cotegl@ncaur.usda.gov
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pubmed:publicationType |
Journal Article
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