Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase.

Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase. Research Abstract Details 

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Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase. Abstract Text:

Hiroshi Tsukamoto,Yoshimitsu Takakura,Toshiki Mine,Takeshi Yamamoto,

A novel bacterium, Photobacterium sp. JT-ISH-224, that produces alpha-/beta-galactoside alpha2,3-sialyltransferase and beta-galactoside alpha2,6-sialyltransferase, was isolated from the gut of a Japanese barracuda. The genes that encode the enzymes were cloned from the genomic library of the bacterium using the genes encoding alpha-/beta-galactoside alpha2,3-sialyltransferase from P. phosphoreum and beta-galactoside alpha2,6-sialyltransferase from P. damselae as probes. The nucleotide sequences were determined, and open reading frames of 1,230 and 1,545 bp for encoding an alpha2,3-sialyltransferase and an alpha2,6-sialyltransferase of 409- and 514-amino acid residues, respectively, were identified. The alpha2,3-sialyltransferase had 92% amino acid sequence identity with the P. phosphoreum alpha2,3-sialyltransferase, whereas the alpha2,6-sialyltransferase had 54% amino acid sequence identity with the P. damselae alpha2,6-sialyltransferase. For both enzymes, the DNA fragments that encoded the full-length protein and its truncated form lacking the putative signal peptide sequence were amplified by a polymerase chain reaction and cloned into an expression vector. Each gene was expressed in Escherichia coli, and the lysate from each strain had enzymatic activity. The alpha2,3-sialyltransferase catalysed the transfer of N-acetylneuraminic acid (NeuAc) from CMP-NeuAc to lactose, alpha-methyl-galactopyranoside and beta-methyl-galactopyranoside with low apparent K(m) and the alpha2,6-sialyltransferase catalysed the transfer of NeuAc from CMP-NeuAc to lactose with low apparent K(m).

Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase. Publishing Authors By Initials

H Tsukamoto,Y Takakura,T Mine,T Yamamoto,

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Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 143

Page Numbers: 187-97

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 4

MONTH: 11

YEAR: 2007

Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase. Keywords Mesh Terms:

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AFFILIATION: Glycotechnology Business Unit, Japan Tobacco Inc., Higashibara, Iwata, Shizuoka 438-0802, Japan.

Country: Japan

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MEDLINETA: J Biochem

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