Glycotechnology Business Unit
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Glycotechnology
Business Unit
JAPAN TOBACCO INC.
c/o Plant Innovation Center
700, Higashibara, Iwata
Shizuoka 438-0802, JAPAN
Fax +81-538-33-6046 |
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We have found a number of novel sialyltransferases from marine bacteria through extensive studies of bacterial glycosylation enzymes. These enzymes have distinctive characteristics absent from mammalian counterparts. We believe that these bacterial enzymes will certainly be useful in synthesis of diverse sialylated compounds and elucidation of biological functions of glycochains.
The acceptor substrate specificity is one of the key differences between bacterial and mammalian sialyltransferases. The Km values of the α2,6-sialyltransferase for lactose, N-acetyllactosaminide and 2'-fucosyllactose are quite similar to each other.
The bacterial α2,3-sialyltransferase transfers N-acetylneuraminic acid residue from CMP-Nue5Ac not only to galactose but also to mannose. We are pleased to offer these bacterial sialyltransferases to the scientific community as research reagents.
Furthermore, we have recently developed a technology to efficiently manufacture 6'-sialyllactose through a research collaboration with Centre National de la Recherche Scientifique in France. The 6'-sialyllactose is produced by a bacterium expressing the α2,6-sialyltransferase. This is a major step toward industrial application of glycoconjugates.
We, Gycobusiness Unit of JAPAN TOBACCO INC., will strive to continue challenges in Glycoworld and would like to make a contribution to the progress of life sciences and society by providing researchers and industries with proprietary glycotechnologies.
Toshiki MINE, Glycobusiness Unit Manager
Enzymes, available
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