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Marine Bacterial Sialyltransferases
Sialyltransferases transfer N-acetylneuraminic acid (Neu5Ac) from the common donor substrate of these enzymes, cytidine 5′-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac), to acceptor substrates. The enzymatic reaction products including sialyl-glycoproteins, sialyl-glycolipids and sialyl-oligosacc...
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Formato: | Texto |
Lenguaje: | English |
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Molecular Diversity Preservation International
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2996176/ https://www.ncbi.nlm.nih.gov/pubmed/21139844 http://dx.doi.org/10.3390/md8112781 |
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author | Yamamoto, Takeshi |
author_facet | Yamamoto, Takeshi |
author_sort | Yamamoto, Takeshi |
collection | PubMed |
description | Sialyltransferases transfer N-acetylneuraminic acid (Neu5Ac) from the common donor substrate of these enzymes, cytidine 5′-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac), to acceptor substrates. The enzymatic reaction products including sialyl-glycoproteins, sialyl-glycolipids and sialyl-oligosaccharides are important molecules in various biological and physiological processes, such as cell-cell recognition, cancer metastasis, and virus infection. Thus, sialyltransferases are thought to be important enzymes in the field of glycobiology. To date, many sialyltransferases and the genes encoding them have been obtained from various sources including mammalian, bacterial and viral sources. During the course of our research, we have detected over 20 bacteria that produce sialyltransferases. Many of the bacteria we isolated from marine environments are classified in the genus Photobacterium or the closely related genus Vibrio. The paper reviews the sialyltransferases obtained mainly from marine bacteria. |
format | Text |
id | pubmed-2996176 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Molecular Diversity Preservation International |
record_format | MEDLINE/PubMed |
spelling | pubmed-29961762010-12-06 Marine Bacterial Sialyltransferases Yamamoto, Takeshi Mar Drugs Review Sialyltransferases transfer N-acetylneuraminic acid (Neu5Ac) from the common donor substrate of these enzymes, cytidine 5′-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac), to acceptor substrates. The enzymatic reaction products including sialyl-glycoproteins, sialyl-glycolipids and sialyl-oligosaccharides are important molecules in various biological and physiological processes, such as cell-cell recognition, cancer metastasis, and virus infection. Thus, sialyltransferases are thought to be important enzymes in the field of glycobiology. To date, many sialyltransferases and the genes encoding them have been obtained from various sources including mammalian, bacterial and viral sources. During the course of our research, we have detected over 20 bacteria that produce sialyltransferases. Many of the bacteria we isolated from marine environments are classified in the genus Photobacterium or the closely related genus Vibrio. The paper reviews the sialyltransferases obtained mainly from marine bacteria. Molecular Diversity Preservation International 2010-11-05 /pmc/articles/PMC2996176/ /pubmed/21139844 http://dx.doi.org/10.3390/md8112781 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Yamamoto, Takeshi Marine Bacterial Sialyltransferases |
title | Marine Bacterial Sialyltransferases |
title_full | Marine Bacterial Sialyltransferases |
title_fullStr | Marine Bacterial Sialyltransferases |
title_full_unstemmed | Marine Bacterial Sialyltransferases |
title_short | Marine Bacterial Sialyltransferases |
title_sort | marine bacterial sialyltransferases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2996176/ https://www.ncbi.nlm.nih.gov/pubmed/21139844 http://dx.doi.org/10.3390/md8112781 |
work_keys_str_mv | AT yamamototakeshi marinebacterialsialyltransferases |