Cargando…
UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections
UDP-GalNAc:polypeptide GalNAc transferase (ppGalNAcT; EC 2.4.1.41) is the initiating enzyme for mucin-type O-glycosylation in animals. Members of this highly conserved glycosyltransferase family catalyse a single glycosidic linkage. They transfer an N-acetylgalactosamine (GalNAc) residue from an act...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer US
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6994419/ https://www.ncbi.nlm.nih.gov/pubmed/31396754 http://dx.doi.org/10.1007/s10719-019-09886-y |
_version_ | 1783493185019838464 |
---|---|
author | Turupcu, Aysegül Poliak, Peter Margreitter, Christian Oostenbrink, Chris Staudacher, Erika |
author_facet | Turupcu, Aysegül Poliak, Peter Margreitter, Christian Oostenbrink, Chris Staudacher, Erika |
author_sort | Turupcu, Aysegül |
collection | PubMed |
description | UDP-GalNAc:polypeptide GalNAc transferase (ppGalNAcT; EC 2.4.1.41) is the initiating enzyme for mucin-type O-glycosylation in animals. Members of this highly conserved glycosyltransferase family catalyse a single glycosidic linkage. They transfer an N-acetylgalactosamine (GalNAc) residue from an activated donor (UDP-GalNAc) to a serine or threonine of an acceptor polypeptide chain. A ppGalNAcT from the freshwater snail Biomphalaria glabrata is the only characterised member of this enzyme family from mollusc origin. In this work, we interpret previously published experimental characterization of this enzyme in the context of in silico models of the enzyme and its acceptor substrates. A homology model of the mollusc ppGalNAcT is created and various substrate peptides are modelled into the active site. We hypothesize about possible molecular interpretations of the available experimental data and offer potential explanations for observed substrate and cofactor specificity. Here, we review and synthesise the current knowledge of Bge-ppGalNAcT, supported by a molecular interpretation of the available data. |
format | Online Article Text |
id | pubmed-6994419 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-69944192020-02-14 UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections Turupcu, Aysegül Poliak, Peter Margreitter, Christian Oostenbrink, Chris Staudacher, Erika Glycoconj J Original Article UDP-GalNAc:polypeptide GalNAc transferase (ppGalNAcT; EC 2.4.1.41) is the initiating enzyme for mucin-type O-glycosylation in animals. Members of this highly conserved glycosyltransferase family catalyse a single glycosidic linkage. They transfer an N-acetylgalactosamine (GalNAc) residue from an activated donor (UDP-GalNAc) to a serine or threonine of an acceptor polypeptide chain. A ppGalNAcT from the freshwater snail Biomphalaria glabrata is the only characterised member of this enzyme family from mollusc origin. In this work, we interpret previously published experimental characterization of this enzyme in the context of in silico models of the enzyme and its acceptor substrates. A homology model of the mollusc ppGalNAcT is created and various substrate peptides are modelled into the active site. We hypothesize about possible molecular interpretations of the available experimental data and offer potential explanations for observed substrate and cofactor specificity. Here, we review and synthesise the current knowledge of Bge-ppGalNAcT, supported by a molecular interpretation of the available data. Springer US 2019-08-08 2020 /pmc/articles/PMC6994419/ /pubmed/31396754 http://dx.doi.org/10.1007/s10719-019-09886-y Text en © The Author(s) 2019 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Original Article Turupcu, Aysegül Poliak, Peter Margreitter, Christian Oostenbrink, Chris Staudacher, Erika UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections |
title | UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections |
title_full | UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections |
title_fullStr | UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections |
title_full_unstemmed | UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections |
title_short | UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata – structural reflections |
title_sort | udp-n-acetyl-α-d-galactosamine:polypeptide n-acetylgalactosaminyltransferase from the snail biomphalaria glabrata – structural reflections |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6994419/ https://www.ncbi.nlm.nih.gov/pubmed/31396754 http://dx.doi.org/10.1007/s10719-019-09886-y |
work_keys_str_mv | AT turupcuaysegul udpnacetyladgalactosaminepolypeptidenacetylgalactosaminyltransferasefromthesnailbiomphalariaglabratastructuralreflections AT poliakpeter udpnacetyladgalactosaminepolypeptidenacetylgalactosaminyltransferasefromthesnailbiomphalariaglabratastructuralreflections AT margreitterchristian udpnacetyladgalactosaminepolypeptidenacetylgalactosaminyltransferasefromthesnailbiomphalariaglabratastructuralreflections AT oostenbrinkchris udpnacetyladgalactosaminepolypeptidenacetylgalactosaminyltransferasefromthesnailbiomphalariaglabratastructuralreflections AT staudachererika udpnacetyladgalactosaminepolypeptidenacetylgalactosaminyltransferasefromthesnailbiomphalariaglabratastructuralreflections |