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dc.contributor.authorBastida, Agatha-
dc.contributor.authorFernández-Mayoralas, Alfonso-
dc.contributor.authorGarcía-Junceda, Eduardo-
dc.identifier.citationBioorganic & Medicinal Chemistry 12(8): 1817-1834 (2002)en_US
dc.description6 pages.-- PMID: 11814863 [PubMed].-
dc.description.abstractRecently we have over-expressed the enzyme a 1,6-fucosyltransferase from Rhizobium sp. in Escherichia coli. In this heterologous system the enzyme was mainly expressed as inclusion bodies and the one that was expressed soluble showed a shortlasting activity in solution due to precipitation of the protein. A structural analysis of the sequence using the TMpred program predicted a highly hydrophobic region of 19 aa close to the C-terminal of the protein. In order to investigate the influence of this region on the formation of inclusion bodies and the precipitation from solution, we cloned a truncated version of the protein where a C-terminal fragment of 65 aa, including the predicted transmembrane-like region, was removed. The resulting protein was expressed in a soluble form without formation of inclusion bodies. The truncated protein catalyzed the transfer of a fucopyranosyl moiety from GDP-b-l-Fucose to chitobiose. Comparison of the acceptor specificity between the truncated a 1,6-fucosyltransferase and the wild-type enzyme, showed a similar behavior for both enzymes. Our results indicate that the active center is not located in the C-terminal extreme of the protein in contrast to the case of the mammalian glycosyltransferases. Also, these results indicate that the a-6-motif III is not directly involved in the catalytic activity of the enzyme.en_US
dc.description.sponsorshipThis work was supported by the Spanish DGES (Grant PB96-0828) and Comunidad de Madrid (Grant 07B/0027/1999).en_US
dc.format.extent458854 bytes-
dc.publisherPergamon Pressen_US
dc.subjectRhizobium Sp.en_US
dc.subjectActivity of the enzymeen_US
dc.titleC-Terminal Truncation of α 1,6-Fucosyltransferase from Rhizobium Sp. does not Annul the Transferase Activity of the Enzymeen_US
dc.description.peerreviewedPeer revieweden_US
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