Effect of C-terminal domain truncation of Thermus thermophilus trehalose synthase on its substrate specificity

Chang Bae Cho, Da Yeon Park, Soo-Bok Lee

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The C-terminal domain of the three-domain-comprising trehalose synthase from Thermus thermophilus was truncated in order to study the effect on the enzyme's activity and substrate specificity. Compared with the wild-type (WT) enzyme, the two truncated enzymes (DM1 and DM2) showed lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism. In the mutants, the glucose moiety cleaved from the maltose substrate was released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose. The WT enzyme, however, retained the glucose in the active site to effectively produce trehalose. In addition, DM1 synthesized much higher amounts of mannose-containing disaccharide trehalose analog (Man-TA) than did the WT and DM2. The results suggest that the C-terminal domain in the WT enzyme is important for retaining the glucose moiety within the active site. The mutant enzymes could be used to produce Man-TA, a postulated inhibitor of gut disaccharidases.

Original languageEnglish
Pages (from-to)121-126
Number of pages6
JournalEnzyme and Microbial Technology
Volume96
DOIs
Publication statusPublished - 2017 Jan 1

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Thermus thermophilus
Substrate Specificity
Trehalose
Enzymes
Substrates
Maltose
Glucose
Catalytic Domain
Disaccharidases
Glucose Oxidase
Glucose oxidase
Disaccharides
Enzyme activity
Mannose
trehalose synthase

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Applied Microbiology and Biotechnology

Cite this

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abstract = "The C-terminal domain of the three-domain-comprising trehalose synthase from Thermus thermophilus was truncated in order to study the effect on the enzyme's activity and substrate specificity. Compared with the wild-type (WT) enzyme, the two truncated enzymes (DM1 and DM2) showed lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism. In the mutants, the glucose moiety cleaved from the maltose substrate was released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose. The WT enzyme, however, retained the glucose in the active site to effectively produce trehalose. In addition, DM1 synthesized much higher amounts of mannose-containing disaccharide trehalose analog (Man-TA) than did the WT and DM2. The results suggest that the C-terminal domain in the WT enzyme is important for retaining the glucose moiety within the active site. The mutant enzymes could be used to produce Man-TA, a postulated inhibitor of gut disaccharidases.",
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Effect of C-terminal domain truncation of Thermus thermophilus trehalose synthase on its substrate specificity. / Cho, Chang Bae; Park, Da Yeon; Lee, Soo-Bok.

In: Enzyme and Microbial Technology, Vol. 96, 01.01.2017, p. 121-126.

Research output: Contribution to journalArticle

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AU - Cho, Chang Bae

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AU - Lee, Soo-Bok

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AB - The C-terminal domain of the three-domain-comprising trehalose synthase from Thermus thermophilus was truncated in order to study the effect on the enzyme's activity and substrate specificity. Compared with the wild-type (WT) enzyme, the two truncated enzymes (DM1 and DM2) showed lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism. In the mutants, the glucose moiety cleaved from the maltose substrate was released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose. The WT enzyme, however, retained the glucose in the active site to effectively produce trehalose. In addition, DM1 synthesized much higher amounts of mannose-containing disaccharide trehalose analog (Man-TA) than did the WT and DM2. The results suggest that the C-terminal domain in the WT enzyme is important for retaining the glucose moiety within the active site. The mutant enzymes could be used to produce Man-TA, a postulated inhibitor of gut disaccharidases.

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