ISSN:
1573-4986
Keywords:
Acceptor specificity
;
α1,3-Fucosyltransferase
;
Key functional group
;
Selectin
;
Sialyl Lewis x
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract To clarify the acceptor specificity of Fuc-TVII, its activity toward various analogs of a 2-(trimethylsilyl)ethyl α2,3-sialyl lacto-N-neotetraose, an acceptor for both Fuc-TVII and Fuc -TVI, was examined in comparison with that of Fuc-TVI. Fuc-TVII required three portions of α2,3-sialylated type-2 oligosaccharide structures (i.e., the hydroxyl group at C-4 of Gal, the hydroxyl group at C-3 of GlcNAc, and the carbonylamino group at C-2 of GlcNAc) for its acceptor recognition. Fuc-TVI required the carbonylamino group at C-2 of GlcNAc for its acceptor recognition. Fuc-TVI I showed higher affinity toward two analogs, in which the hydroxyl group at C-6 of GlcNAc has been deoxygenated and the acetamide group of N-acetylneuraminic acid has been replaced with a glycolylamino group, respectively, than that toward the original compound. On the other hand, Fuc-TVI showed higher affinity toward an analog, in which the acetamide group of GlcNAc has been modified with a lauroylamino group, than that toward the original compound. Analysis involving mass spectrometry confirmed that both Fuc-TVII and Fuc-TVI could fucosylate these three analogs to yield sialyl Lewis x derivatives.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1006933808303
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