Mar. Drugs 2010, 8(11), 2781-2794; doi:10.3390/md8112781
Review

Marine Bacterial Sialyltransferases

Glycotechnology Business Unit, Japan Tobacco Inc., 700 Higashibara, Iwata, Shizuoka 438-0802, Japan
Received: 20 September 2010; in revised form: 25 October 2010 / Accepted: 2 November 2010 / Published: 5 November 2010
(This article belongs to the Special Issue Enzymes from the Sea: Sources, Molecular Biology and Bioprocesses)
PDF Full-text Download PDF Full-Text [301 KB, uploaded 5 November 2010 15:31 CET]
Abstract: 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.
Keywords: marine bacteria; Photobacterium; sialyltransferase; sialic acid

Article Statistics

Load and display the download statistics.

Citations to this Article

Cite This Article

MDPI and ACS Style

Yamamoto, T. Marine Bacterial Sialyltransferases. Mar. Drugs 2010, 8, 2781-2794.

AMA Style

Yamamoto T. Marine Bacterial Sialyltransferases. Marine Drugs. 2010; 8(11):2781-2794.

Chicago/Turabian Style

Yamamoto, Takeshi. 2010. "Marine Bacterial Sialyltransferases." Mar. Drugs 8, no. 11: 2781-2794.

Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert