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
| Autor: | Takeshi Yamamoto, Toshiki Mine, Katsumi Ajisaka, Naoya Tateda, Hitomi Kajiwara, Tatsuo Miyazaki |
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| Rok vydání: | 2010 |
| Předmět: |
beta-Galactoside alpha-2
3-Sialyltransferase Stereochemistry Sialyltransferase Biochemistry Substrate Specificity Analytical Chemistry chemistry.chemical_compound Moiety chemistry.chemical_classification biology Photobacterium Organic Chemistry Stereoisomerism Cytidine General Medicine Nuclear magnetic resonance spectroscopy biology.organism_classification Acceptor N-Acetylneuraminic Acid Recombinant Proteins Sialyltransferases Enzyme chemistry biology.protein N-Acetylneuraminic acid Inositol |
| Zdroj: | Carbohydrate Research. 345:2485-2490 |
| ISSN: | 0008-6215 |
| Popis: | 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-, 1 d -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. |
| Databáze: | OpenAIRE |
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