Literature DB >> 11229321

Molecular cloning of cDNA encoding N-acetylglucosaminyltransferase II from Arabidopsis thaliana.

R Strasser1, H Steinkellner, M Borén, F Altmann, L Mach, J Glössl, J Mucha.   

Abstract

N-acetylglucosaminyltransferase II (GnTII, EC 2.4.1.143) is a Golgi enzyme involved in the biosynthesis of glycoprotein-bound N-linked oligosaccharides, catalysing an essential step in the conversion of oligomannose-type to complex N-glycans. GnTII activity has been detected in both animals and plants. However, while cDNAs encoding the enzyme have already been cloned from several mammalian sources no GnTII homologue has been cloned from plants so far. Here we report the molecular cloning of an Arabidopsis thaliana GnTII cDNA with striking homology to its animal counterparts. The predicted domain structure of A. thaliana GnTII indicates a type II transmembrane protein topology as it has been established for the mammalian variants of the enzyme. Upon expression of A. thaliana GnTII cDNA in the baculovirus/insect cell system, a recombinant protein was produced that exhibited GnTII activity.

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Year:  1999        PMID： 11229321     DOI： 10.1023/a:1007127815012

Source DB:  PubMed          Journal:  Glycoconj J        ISSN： 0282-0080            Impact factor:   2.916


  15 in total

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5.  Molecular cloning and characterization of cDNA coding for beta1, 2N-acetylglucosaminyltransferase I (GlcNAc-TI) from Nicotiana tabacum.

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  19 in total

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7.  Two closely related forms of UDP-GlcNAc: alpha6-D-mannoside beta1,2-N-acetylglucosaminyltransferase II occur in the clawed frog Xenopus laevis.

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