Crystal structure of α

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• 作者：Toru Iwatani ; Nozomu Okino ; Mai Sakakura ; Hitomi Kajiwara ; Yoshimitsu Takakura ; Makoto Kimura ; Makoto Ito ; Takeshi Yamamoto ; Yoshimitsu Kakuta
• 关键词：α ; 2 ; 3-Sialyltransfease ; Crystal structure ; JT-ISH-467 ; Sialic acid ; Broad substrate specificity ; Active conformation ; Photobacterium phosphoreum
• 刊名：FEBS Letters
• 出版年：2009
• 出版时间：18 June 2009
• 年：2009
• 卷：583
• 期：12
• 页码：2083-2087
• 全文大小：452 K

文摘

α/β-Galactoside α2,3-sialyltransferase produced by Photobacterium phosphoreum JT-ISH-467 is a unique enzyme that catalyzes the transfer of N-acetylneuraminic acid residue from cytidine monophosphate N-acetylneuraminic acid to acceptor carbohydrate groups. The enzyme recognizes both mono- and di-saccharides as acceptor substrates, and can transfer Neu5Ac to both α-galactoside and β-galactoside, efficiently. To elucidate the structural basis for the broad acceptor substrate specificity, we determined the crystal structure of the α2,3-sialyltransferase in complex with CMP. The overall structure belongs to the glycosyltransferase-B structural group. We could model a reasonable active conformation structure based on the crystal structure. The predicted structure suggested that the broad substrate specificity could be attributed to the wider entrance of the acceptor substrate binding site.