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KMID : 1007520020110060640
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Food Science and Biotechnology
2002 Volume.11 No. 6 p.640 ~ p.643
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Tyr260 Residue in Bacillus macerans Cyclodextrin Glucanotransferase
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Kim, Chang Sup
Han, Nam Soo/Keum, Inkyung/Tao, Bernard Y./Seo, Jin-Ho
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Abstract
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Site-directed mutagenesis was performed at nucleotides corresponding the Tyr260 residue of the Bacillus macerans cyclodextrin glucanotransferase. The mutant enzyme retained measurable hydrolytic activity compared with that of the wild-type. Cylization activity was not detcted after a long period of the enzyme reaction. The result gives an insight that Tyr260 residue contributes to cyclization reaction of the enzyme. Comparative analysis of the primary sequence alignment indicates that the residue constitutes subsite ＋2, forming a nonpolar stacking interaction with sugar.
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