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Site-directed mutagenesis of possible catalytic residues of cellobiose 2-epimerase from Ruminococcus albus

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タイトル: Site-directed mutagenesis of possible catalytic residues of cellobiose 2-epimerase from Ruminococcus albus
著者: Ito, Shigeaki 著作を一覧する
Hamada, Shigeki 著作を一覧する
Ito, Hiroyuki 著作を一覧する
Matsui, Hirokazu 著作を一覧する
Ozawa, Tadahiro 著作を一覧する
Taguchi, Hidenori 著作を一覧する
Ito, Susumu 著作を一覧する
キーワード: Cellobiose 2-epimerase
Ruminococcus albus
Homology modeling
Site-directed mutagenesis
発行日: 2009年 7月
出版者: Springer Netherlands
誌名: Biotechnology Letters
巻: 31
号: 7
開始ページ: 1065
終了ページ: 1071
出版社 DOI: 10.1007/s10529-009-9979-3
抄録: Cellobiose 2-epimerase (EC from Ruminococcus albus (RaCE) catalyzes the reversible epimerization of cellobiose and lactose to 4-O-β-D-glucopyranosyl-D-mannose and 4-O-β-D-galactopyranosyl-D-mannose (epilactose). Based on the structure-based amino acid sequence alignment with N-acetyl-D-glucosamine 2-epimerases (EC from porcine kidney and Anabaena sp. CH1 and on the computer-aided model building of the tertiary structure of RaCE, we performed site-directed mutagenesis of possible catalytic residues in the enzyme, and the mutants were expressed in Escherichia coli cells. It was found that R52, H243, E246, W249, M251, W304, E308, H374, and M378 were absolutely required for the activity of RaCE. F114 and W303 (and possibly R377) also contributed to catalysis. These possible catalytic protruded into or near the active-site cleft surrounded by the inner α-helices in the predicted (α/α)6 core barrel structure of RaCE.
Rights: The original publication is available at
資料タイプ: article (author version)
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 伊藤 進


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