Identification of Amino-Acids Residues for Key Role in Dextransucrase Activity of Leuconostoc mesenteroides B-742CB
2004
Ryu, H.J. (Chonnam National University, Gwangju, Republic of Korea) | Yoon, S.H. (Iowa State University, Ames, IA, U.S.A.) | Kim, D.W. (Kangnung National University, Kangnung, Republic of Korea) | Chang, S.S. (Pohang University of Science and Technology, Pohang, Republic of Korea) | Kim, S.H. (Lifenza Co., Ltd., Seoul, Republic of Korea) | Kimura, Atsuo (Hokkaido University, Sapporo, Japan) | Kim, D.M. (Chonnam National University, Gwangju, Republic of Korea), E-mail: [email protected] | Seo, E.S. (Chonnam National University, Gwangju, Republic of Korea) | Kang, H.K. (Chonnam National University, Gwangju, Republic of Korea) | Lee, J.H. (Chonnam National University, Gwangju, Republic of Korea) | Cho, J.Y. (Chonnam National University, Gwangju, Republic of Korea) | Robyt John F. (Iowa State University, Ames, IA, U.S.A.)
Dextransucrase (DSRB742) from Leuconostoc mesenteroides NRRL B-742CB is a glucosyltransferase that catalyzes the synthesis of dextran using sucrose, or the synthesis of oligosaccharides when acceptor molecules, like maltose, are present. The DSRB742 gene (dsrB742) was cloned and the properties were characterized. In order to identify critical amino acid residues, the DSRB742 amino acid sequence was aligned with glucosyltransferase sequences, and three amino acid residues reported as sucrose binding amino acids in Streptococcus glucosyltransferases were selected for site-directed mutagenesis experiments.
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