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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Main Author: Takeshi Yamamoto
Format: Article
Language:English
Published: MDPI AG 2010-11-01
Series:Marine Drugs
Subjects:
Online Access:http://www.mdpi.com/1660-3397/8/11/2781/
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spelling doaj-c5496ccbe8424cb6aa6a25fe6f6311d42020-11-24T23:25:43ZengMDPI AGMarine Drugs1660-33972010-11-018112781279410.3390/md8112781Marine Bacterial SialyltransferasesTakeshi YamamotoSialyltransferases 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. http://www.mdpi.com/1660-3397/8/11/2781/marine bacteriaPhotobacteriumsialyltransferasesialic acid
collection DOAJ
language English
format Article
sources DOAJ
author Takeshi Yamamoto
spellingShingle Takeshi Yamamoto
Marine Bacterial Sialyltransferases
Marine Drugs
marine bacteria
Photobacterium
sialyltransferase
sialic acid
author_facet Takeshi Yamamoto
author_sort Takeshi Yamamoto
title Marine Bacterial Sialyltransferases
title_short Marine Bacterial Sialyltransferases
title_full Marine Bacterial Sialyltransferases
title_fullStr Marine Bacterial Sialyltransferases
title_full_unstemmed Marine Bacterial Sialyltransferases
title_sort marine bacterial sialyltransferases
publisher MDPI AG
series Marine Drugs
issn 1660-3397
publishDate 2010-11-01
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.
topic marine bacteria
Photobacterium
sialyltransferase
sialic acid
url http://www.mdpi.com/1660-3397/8/11/2781/
work_keys_str_mv AT takeshiyamamoto marinebacterialsialyltransferases
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