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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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Detalles Bibliográficos
Autor principal: Yamamoto, Takeshi
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2010
Materias:
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.
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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