The specificity of an alpha-(1-->2)-L-galactosyltransferase from albumen glands of the snail Helix pomatia.

2)-L-galactosyltransferase from albumen glands of the snail Helix pomatia. -->
Autoři: Lüttge H; Zoologisches Institut und Zoologisches Museum, Hamburg, Germany., Heidelberg T, Stangier K, Thiem J, Bretting H
Zdroj: Carbohydrate research [Carbohydr Res] 1997 Jan 17; Vol. 297 (3), pp. 281-8.
Způsob vydávání: Journal Article; Research Support, Non-U.S. Gov't
Jazyk: English
Informace o časopise: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 0043535 Publication Model: Print Cited Medium: Print ISSN: 0008-6215 (Print) Linking ISSN: 00086215 NLM ISO Abbreviation: Carbohydr Res Subsets: MEDLINE
Imprint Name(s): Publication: Amsterdam : Elsevier
Original Publication: Amsterdam.
Výrazy ze slovníku MeSH: Galactosyltransferases/*metabolism , Helix, Snails/*enzymology, Animals ; Chromatography, Gas ; Chromatography, Thin Layer ; Disaccharides/chemical synthesis ; Fucose/metabolism ; Galactose/metabolism ; Magnetic Resonance Spectroscopy ; Substrate Specificity ; Trisaccharides/chemical synthesis
Abstrakt: The specificity of an L-galactosyltransferase (L-Gal-T) from albumen glands of the snail Helix pomatia has been studied. This enzyme transfers L-Gal from GDP-L-Gal to various disaccharides with beta-linked D-Gal in terminal non-reducing position, forming an alpha-(1-->2) linkage. The subterminal residue and the type of interglycosidie linkage proved to be of minor importance. However, the branched trisaccharide beta-D-Gal-(1-->3)-[beta-D-Gal-(1-->6)]-beta-D-Gal-(1-->O)Me is a very poor acceptor. The specificity of the L-Gal-T correlates well with the equimolar occurrence of L-Gal and the structural element-->2)-Gal- (1-->found in the storage polysaccharide of this snail. Since L-Fuc is also transferred from its GDP-activated form, the membrane preparations of the albumen glands can be used to synthesize fucosylated oligosaccharides.
Substance Nomenclature: 0 (Disaccharides)
0 (Trisaccharides)
28RYY2IV3F (Fucose)
EC 2.4.1.- (Galactosyltransferases)
X2RN3Q8DNE (Galactose)
Entry Date(s): Date Created: 19970117 Date Completed: 19970609 Latest Revision: 20191210
Update Code: 20231215
DOI: 10.1016/s0008-6215(96)00277-7
PMID: 9060190
Autor: Lüttge H; Zoologisches Institut und Zoologisches Museum, Hamburg, Germany., Heidelberg T, Stangier K, Thiem J, Bretting H
Jazyk: angličtina
Zdroj: Carbohydrate research [Carbohydr Res] 1997 Jan 17; Vol. 297 (3), pp. 281-8.
DOI: 10.1016/s0008-6215(96)00277-7
Abstrakt: The specificity of an L-galactosyltransferase (L-Gal-T) from albumen glands of the snail Helix pomatia has been studied. This enzyme transfers L-Gal from GDP-L-Gal to various disaccharides with beta-linked D-Gal in terminal non-reducing position, forming an alpha-(1-->2) linkage. The subterminal residue and the type of interglycosidie linkage proved to be of minor importance. However, the branched trisaccharide beta-D-Gal-(1-->3)-[beta-D-Gal-(1-->6)]-beta-D-Gal-(1-->O)Me is a very poor acceptor. The specificity of the L-Gal-T correlates well with the equimolar occurrence of L-Gal and the structural element-->2)-Gal- (1-->found in the storage polysaccharide of this snail. Since L-Fuc is also transferred from its GDP-activated form, the membrane preparations of the albumen glands can be used to synthesize fucosylated oligosaccharides.
Databáze: MEDLINE
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