Publication
N-acetylglucosamine-1-phosphate transferase, alpha/beta and gamma subunits; N-acetylglucosamine-1- (GNPTAB, GNPTG)
| dc.contributor.author | Coutinho, Maria Francisca | |
| dc.date.accessioned | 2014-04-11T12:34:14Z | |
| dc.date.available | 2014-04-11T12:34:14Z | |
| dc.date.issued | 2014-05 | |
| dc.description.abstract | GlcNAc-1-phosphotransferase catalyzes the transfer of a GlcNAc-1-phosphate residue from UDP-GlcNAc to C6 positions of selected mannoses in highmannose- type oligosaccharides of the hydrolases (Goldberg and Kornfeld 1981; Natowicz et al. 1982; Varki and Kornfeld 1983). At a biological level this reaction is followed by the removal of the terminal GlcNAc by an N-acetylglucosamine-1-phosphodiester α-N-acetyl-glucosaminidase, usually referred to as “uncovering enzyme” (UCE; see Chap. 78; Article ID: 332135). Sequential action of these two enzymes results in the formation of the mannose-6-phosphate (Man-6-P) marker, a specific tag acquired by lysosomal hydrolases that ensures recognition by M6P receptors and delivery to the endosomal/lysosomal system (Braulke and Bonifacino 2009). | por |
| dc.identifier.citation | In: Taniguchi N, Honke K, Fukuda M, et al. (eds). Handbook of Glycosyltransferases and Related Genes. Tokyo: Springer-Verlag, 2014 | por |
| dc.identifier.issn | 0959-6658 | |
| dc.identifier.uri | http://hdl.handle.net/10400.18/2244 | |
| dc.language.iso | eng | por |
| dc.peerreviewed | yes | por |
| dc.publisher | Springer-Verlag | por |
| dc.relation.publisherversion | http://www.springerreference.com/index/chapterdbid/332158 | por |
| dc.subject | Doenças Genéticas | por |
| dc.subject | N-acetylglucosamine-1-phosphate transferase | por |
| dc.title | N-acetylglucosamine-1-phosphate transferase, alpha/beta and gamma subunits; N-acetylglucosamine-1- (GNPTAB, GNPTG) | por |
| dc.type | book part | |
| dspace.entity.type | Publication | |
| oaire.citation.title | Handbook of Glycosyltransferases and Related Genes | por |
| rcaap.rights | restrictedAccess | por |
| rcaap.type | bookPart | por |
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