| Substrate specificity of GM2 and GD3 synthase of Golgi vesicles derived from rat liver. | |
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MedLine Citation:
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PMID: 3115774 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Several GM3 derivatives have been synthesized. Among them were lyso-GM3 derivatives and GM3 analogues with modifications in the sialic acid moiety. They were used as glycolipid acceptors in assays for GM2 and GD3 synthase of rat liver Golgi. Analysis of the resulting enzyme activities and of the reaction products revealed different substrate specificities for GM2 and GD3 synthase although the normal glycolipid acceptor for both transferases is ganglioside GM3. Specificity of GD3 synthase is strongly determined by the substrate's negative charge and the acyl residue in amide bond to the amino group of neuraminic acid, while GM2 synthase reacts quite indifferently to these changes in the sialic moiety of the substrate. Both enzymes seem to be sensitive to the spatial extension at the neuraminic acid's carboxylic group. |
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Authors:
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D Klein; G Pohlentz; G Schwarzmann; K Sandhoff |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 167 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1987 Sep |
Date Detail:
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Created Date: 1987-11-16 Completed Date: 1987-11-16 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY, WEST |
Other Details:
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Languages: eng Pagination: 417-24 Citation Subset: IM |
Affiliation:
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Institut für Organische Chemie und Biochemie, Universität Bonn, Federal Republic of Germany. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Carbohydrate Conformation Carbohydrate Sequence Chromatography, Thin Layer Galactosyltransferases / metabolism* Golgi Apparatus / enzymology* Liver / enzymology* Mass Spectrometry N-Acetylgalactosaminyltransferases* Rats Sialyltransferases / metabolism* Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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EC 2.4.1.-/Galactosyltransferases; EC 2.4.1.-/N-Acetylgalactosaminyltransferases; EC 2.4.1.-/UDP-GalNAc-beta-galactose beta 1,4-N-acetylgalactosaminyltransferase; EC 2.4.1.92/(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase; EC 2.4.99.-/Sialyltransferases; EC 2.4.99.8/alpha-N-acetylneuraminate alpha-2,8-sialyltransferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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