Detailed acceptor specificities of human alpha1,3-fucosyltransferases, Fuc-TVII and Fuc-TVI.
To clarify the acceptor specificity of Fuc-TVII, its activity toward various analogs of a 2-(trimethylsilyl)ethyl alpha2,3-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 alpha2,3-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-TVII 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.
Shinoda
K
K
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Tokyo, Japan. katsumi.shinoda@kyowa.co.jp
Tanahashi
E
E
Fukunaga
K
K
Ishida
H
H
Kiso
M
M
D001667:Binding, Competitive; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005647:Fucosyltransferases / Q000378:metabolism*; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D009844:Oligosaccharides; D005647:Fucosyltransferases; C031692:galactoside 3-fucosyltransferase