A recombinant α-(2→3)-sialyltransferase with an extremely broad acceptor substrate specificity from Photobacterium sp. JT-ISH-224 can transfer N-acetylneuraminic acid to inositols.
We confirmed that a recombinant α-(2→3)-sialyltransferase cloned from Photobacterium sp. JT-ISH-224 recognizes inositols having a structure corresponding to the C-3 and C-4 of a galactopyranoside moiety, such as epi-, 1d-chiro, myo-, and muco-inositol, as acceptor substrates, and that the enzyme can transfer N-acetylneuraminic acid (Neu5Ac) from cytidine 5'-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac) to them. After purifying the reaction products, the structures were confirmed by use of NMR spectroscopy and mass spectrometry. From these results, it was clearly shown that the α-(2→3)-sialyltransferase from Photobacterium sp. JT-ISH-224 recognizes acceptor substrates through the cis-diol structure corresponding to the 3- and 4-position of the galactopyranoside moiety.
Glycotechnology Business Unit, Japan Tobacco Inc., 700 Higashibara, Iwata, Shizuoka 438-0802, Japan. toshiki.mine@jt.com
Toshiki
T
Mine
Tatsuo
T
Miyazaki
Hitomi
H
Kajiwara
Naoya
N
Tateda
Katsumi
K
Ajisaka
Takeshi
T
Yamamoto
D007294:Inositol / Q000737:chemistry / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid / Q000737:chemistry / Q000378:metabolism*; D010776:Photobacterium / Q000201:enzymology*; D011994:Recombinant Proteins / Q000378:metabolism*; D012799:Sialyltransferases / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase
D011994:Recombinant Proteins; D007294:Inositol; D012799:Sialyltransferases; D019158:N-Acetylneuraminic Acid; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase