Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase

Inhibitory effects on several disaccharidase activities

Hye Min Kim, You Kyung Chang, Soo In Ryu, Sung Gweon Moon, Soo-Bok Lee

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase employed a galactose as an acceptor in the glucosyl transfer reaction with an NDP-Glc donor. The reaction produced a non-reducing transfer product in a yield of more than 30% based on the molar concentration of donor used. The transfer product was purified by paper chromatography and preparative HPLC, and its glycosidic structure was confirmed by 13C nuclear magnetic resonance to be α-d-glucopyranosyl α-d-galactopyranoside. Interestingly, this trehalose analogue disaccharide inhibited the action of several disaccharidases, including a trehalase. The analogue competitively inhibited porcine kidney and rat intestinal trehalases with Ki values of 0.68 and 3.7 mM, respectively. It also competitively inhibited other intestinal disaccharidases such as sucrase, maltase, and isomaltase with respective Ki values of approximately 0.66, 3.0, and 2.1 mM. Accordingly, this trehalose analogue would be a potentially indigestible disaccharide, effectively inhibiting intestinal brush border disaccharidases.

Original languageEnglish
Pages (from-to)98-103
Number of pages6
JournalJournal of Molecular Catalysis B: Enzymatic
Volume49
Issue number1-4
DOIs
Publication statusPublished - 2007 Nov 16

Fingerprint

Pyrococcus horikoshii
Disaccharidases
Glycosyltransferases
Trehalose
Disaccharides
Galactose
Trehalase
Paper Chromatography
Brushes
Microvilli
Chromatography
Rats
Magnetic Resonance Spectroscopy
Swine
High Pressure Liquid Chromatography
Nuclear magnetic resonance
Kidney

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Catalysis
  • Process Chemistry and Technology

Cite this

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title = "Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities",
abstract = "Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase employed a galactose as an acceptor in the glucosyl transfer reaction with an NDP-Glc donor. The reaction produced a non-reducing transfer product in a yield of more than 30{\%} based on the molar concentration of donor used. The transfer product was purified by paper chromatography and preparative HPLC, and its glycosidic structure was confirmed by 13C nuclear magnetic resonance to be α-d-glucopyranosyl α-d-galactopyranoside. Interestingly, this trehalose analogue disaccharide inhibited the action of several disaccharidases, including a trehalase. The analogue competitively inhibited porcine kidney and rat intestinal trehalases with Ki values of 0.68 and 3.7 mM, respectively. It also competitively inhibited other intestinal disaccharidases such as sucrase, maltase, and isomaltase with respective Ki values of approximately 0.66, 3.0, and 2.1 mM. Accordingly, this trehalose analogue would be a potentially indigestible disaccharide, effectively inhibiting intestinal brush border disaccharidases.",
author = "Kim, {Hye Min} and Chang, {You Kyung} and Ryu, {Soo In} and Moon, {Sung Gweon} and Soo-Bok Lee",
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AU - Chang, You Kyung

AU - Ryu, Soo In

AU - Moon, Sung Gweon

AU - Lee, Soo-Bok

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AB - Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase employed a galactose as an acceptor in the glucosyl transfer reaction with an NDP-Glc donor. The reaction produced a non-reducing transfer product in a yield of more than 30% based on the molar concentration of donor used. The transfer product was purified by paper chromatography and preparative HPLC, and its glycosidic structure was confirmed by 13C nuclear magnetic resonance to be α-d-glucopyranosyl α-d-galactopyranoside. Interestingly, this trehalose analogue disaccharide inhibited the action of several disaccharidases, including a trehalase. The analogue competitively inhibited porcine kidney and rat intestinal trehalases with Ki values of 0.68 and 3.7 mM, respectively. It also competitively inhibited other intestinal disaccharidases such as sucrase, maltase, and isomaltase with respective Ki values of approximately 0.66, 3.0, and 2.1 mM. Accordingly, this trehalose analogue would be a potentially indigestible disaccharide, effectively inhibiting intestinal brush border disaccharidases.

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