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D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major
In this work we describe an unusual enzyme from Leishmania major (Arabinokinase/Pyrophosphorylase) that catalyzes the synthesis of GDP-D-arabinopyranose (GDP-D-Arap) via a D-arabinose-1-phosphate intermediate in the presence of ATP and GTP. Our data indicate GDP-D-Arap transport in vivo by the LPG2...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
A.I. Gordeyev
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347535/ https://www.ncbi.nlm.nih.gov/pubmed/22649617 |
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author | Novozhilova, N.M. Bovin, N.V. |
author_facet | Novozhilova, N.M. Bovin, N.V. |
author_sort | Novozhilova, N.M. |
collection | PubMed |
description | In this work we describe an unusual enzyme from Leishmania major (Arabinokinase/Pyrophosphorylase) that catalyzes the synthesis of GDP-D-arabinopyranose (GDP-D-Arap) via a D-arabinose-1-phosphate intermediate in the presence of ATP and GTP. Our data indicate GDP-D-Arap transport in vivo by the LPG2 multispecific nucleotide sugar transporter into the Leishmania Golgi apparatus, in which it can be used by glycosyltransferases as a donor substrate for glycosylation. |
format | Online Article Text |
id | pubmed-3347535 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | A.I. Gordeyev |
record_format | MEDLINE/PubMed |
spelling | pubmed-33475352012-05-30 D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major Novozhilova, N.M. Bovin, N.V. Acta Naturae Research Article In this work we describe an unusual enzyme from Leishmania major (Arabinokinase/Pyrophosphorylase) that catalyzes the synthesis of GDP-D-arabinopyranose (GDP-D-Arap) via a D-arabinose-1-phosphate intermediate in the presence of ATP and GTP. Our data indicate GDP-D-Arap transport in vivo by the LPG2 multispecific nucleotide sugar transporter into the Leishmania Golgi apparatus, in which it can be used by glycosyltransferases as a donor substrate for glycosylation. A.I. Gordeyev 2009-10 /pmc/articles/PMC3347535/ /pubmed/22649617 Text en Copyright © 2009 Park-media Ltd. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Novozhilova, N.M. Bovin, N.V. D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major |
title | D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major |
title_full | D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major |
title_fullStr | D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major |
title_full_unstemmed | D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major |
title_short | D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major |
title_sort | d-arabinose methabolism: characterization of bifunctional arabinokinase/pyrophosphorylase of leishmania major |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347535/ https://www.ncbi.nlm.nih.gov/pubmed/22649617 |
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