The study of the substrate specificity of rat-brain fucosyltransferase using synthetic acceptors |
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| Authors: | G. Ya. Wiederschain O. Koul N. V. Bovin N. E. Nifant’ev R. McCluer |
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| Affiliation: | (1) Department of Biomedical Sciences, E.K. Shriver Center, 02452 Waltham, MA;(2) Departments of Neurology, Massachusetts General Hospital and Harvard Medical School, 02115 Boston, MA, USA;(3) Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117871 GSP-7, Moscow, Russia;(4) Zelinskii Institute of Organic Chemistry, Russian Academy of Sciences, Leninskii pr. 47, 117913 GSP-1 Moscow, Russia;(5) Department of Pediatrics, University of Texas Medical School, 77030 Houston, TX, USA |
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| Abstract: | The substrate specificity of fucosyltransferase (FT) from rat forebrain and cerebellum was studied using synthetic acceptors. Of 16 acceptors tested, only those containing the Galβ1-4GlcNAcβ1-R fragment were subjected to enzymic fucosylation. The isomer with a 1–3 bond as well as lactose and oligosaccharides with an additional Neu5Ac residue attached to Gal or a Fuc residue attached to GlcNAc were not fucosylated, whereas Fucα1-2Galβ1-4GlcNAc displayed the same substrate properties as Galβ1-4GlcNAc. FT from the cerebellum and forebrain was shown to have a specificity similar to that of mammalian FT IV. The activity of the cerebellum FT with all types of substrates was higher than that of FT isolated from the forebrain, the specificity profiles being similar. This communication is dedicated to the 70th birthday of Prof. A.Ya. Khorlin. |
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| Keywords: | fucosyltransferase substrate specificity synthetic acceptors rat brain |
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