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Inhibition by maltose, isomaltose, and nigerose of the synthesis of high-molecular-weight d-glucans by the d- glucosyltransferases of Streptococcus sobrinus

✍ Scribed by David McAlister; R. Jennings Doyle; K. Grant Taylor

Book ID: 102995573
Publisher: Elsevier Science
Year: 1989
Tongue: English
Weight: 577 KB
Volume: 187
Category: Article
ISSN: 0008-6215
DOI: 10.1016/0008-6215(89)80060-6

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✦ Synopsis

Two D-ghtcosyltransferases are produced by Streptococcus sobrinus C211. One (GTF-S) catalyzes the conversion of sucrose into soluble a-(l-6)-linked (Y-(l-+3)-branched D-glucans, and the other (GTF-I), of sucrose into a-(l-+3)-linked a-(l-+6)-branched

D-glucans. These enzymes were studied by using maltose, isomaltose, and nigerose as inhibitors. Maltose and isomaltose were found to be competitive inhibitors of GTF-S, whereas nigerose has no effect on GTF-S activity, The Ki values for maltose and isomaltose were determined to be 11 and lSmM, respectively.

Maltose, isomaltose, and nigerose competitively inhibit GTF-I. The Ki values for these inhibitors were found to be -0.8, 2.5, and 15mM, respectively.

The inhibitory properties of each disaccharide are interpreted in terms of conformational comparisons with sucrose.

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