Purification, crystallization and preliminary crystallographic characterization of the α2,6-sialyltransferase from<i>Photobacterium</i>sp. JT-ISH-224

Okino, Nozomu; Kakuta, Yoshimitsu; Kajiwara, Hitomi; Ichikawa, Masaki; Takakura, Yoshimitsu; Ito, Makoto; Yamamoto, Takeshi

doi:10.1107/s1744309107031363

Cited by 5 publications

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“…We have reported several kinds of the nucleotide sequence encoding marine bacterial sialyltransferases obtained from P. damselae, 9) P. phosphoreum, 10) P. leiog- nathi, 11) Photobacterium sp. 12) and Vibrio sp. 13) The result of multiple alignments among the marine bacterial sialyltransferases is shown in Fig.…”

Section: Multiple Alignments Among the Marine Bacterial Sialyltransfementioning

confidence: 99%

Sialyltransferases Obtained from Marine Bacteria

Kajiwara¹,

Mine²,

Yamamoto³

2009

J. Appl. Glycosci.

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Sialic acids (Sias) are important components of carbohydrate chains and are linked to terminal positions of the carbohydrate moiety of glycoconjugates, including glycoproteins and glycolipids. 1) A lot of studies have focused on clarifying the structure function relationship of Sias and have revealed that N acetylneuraminic acid (Neu5Ac) is the major Sia component of glycoconjugates, and that the sialylated glycoconjugates play significant roles in many biological processes. 2) In the sialylated glycoconjugates, mainly four linkage patterns, including Neu5Acα2 6Gal, Neu5Acα2 3Gal, Neu5Acα2 6GalNAc and Neu5Acα2 8Neu5Ac are found. 1,2) These structures are formed by specific sialyltransferases in the cell. Therefore, the sialyltransferases are considered key enzymes in the biosynthesis and in vitro enzymatic synthesis of sialylated glycoconjugates and or glycans. Here, all known sialyltransferases use cytidine 5 monophosphate N acetylneuraminic acid (CMP Neu5Ac) as the common donor substrate. 2) The sialyltransferases have been cloned from various sources, including mammalian organs, viruses and bacteria. 1,3,4) Generally, the enzymes from a bacteria are more stable and productive in Escherichia coli protein expression systems than the mammalian derived enzymes. These advantages highlight the capacity of bacterial enzymes as efficient tools for the in vitro enzymatic synthesis of sialosides. Genes encoding sialyltransferases have been cloned from various types of bacteria, including Neisseria gonorrhoeae, 5) Neisseria meningitidis, 6) Campylobacter jejuni, 7) E. coli, 8) Photobacterium damselae, 9) Photobacterium phosphoreum, 10) Photobacterium leiognathi, 11) Photobacterium sp., 12) Vibrio sp., 13) Pasteurella multocida, 14) Haemophilus influenzae 15) and Streptococcus agalactiae. 16) All the sialyltransferases, including mammalian, viral and bacterial origin, have been classified into five families in the CAZy database. However, all bacterial sialyltransferases are classified into four families in the CAZy database: 17) (1) glycosyltransferase (GT) family 38 (polysialyltransferase from E. coli and N. meningitidis); (2) GT family 42 (lipooligosaccharide α2,3 sialyltransferase and α2,3 α 2,8 sialyltransferase from C. jejuni and H. influenzae); (3) GT family 52 (α2,3 sialyltransferase from H. influenzae, N. gonorrhoeae and N. meningitidis) and (4) GT family 80 (α2,6 sialyltransferase and α2,3 α2,6 sialyltransferase from P. damselae and P. multocida). An abundant supply of sialylated oligosaccharides is essential for investigation of the biological function of sialylation. Enzymatic glycosylation using glycosyltransferases is a single step process with high positional and anomer selectivity and high reaction yield. For example, with sialylation, the transfer of Neu5Ac by sialyltransferases to the appropriate substrate from CMP Neu5Ac as the donor substrate can be readily achieved in the final step under mild reaction conditions. 18) Therefore, sialyltransferases are thought to be a powerful tool for the study of glyc...

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