Catalytic reversibility of Pyrococcus horikoshii trehalose synthase

Efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling

Soo In Ryu, Jeong Eun Kim, Eun Joo Kim, Seung Kyung Chung, Soo-Bok Lee

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The trehalose synthase (TreT) from Pyrococcus horikoshii represented reversible catalysis in alternative synthesis of trehalose and nucleoside 5′-diphosphate-glucose (NDP-Glc), depending on the substrates involved. TreT from P. horikoshii had differential preferences on NDP-Glc as a donor for trehalose synthesis, in which guanosine 5′-diphosphate (GDP)-Glc was the most favored in terms of reaction specificity, kcat/Km. Uridine 5′-diphosphate (UDP)- and adenosine 5′-diphosphate (ADP)-Glcs were employed with less preferences. This enzyme reversely cleaved trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-Glcs. Although ADP-Glc was the least favorable donor, the counterpart, ADP, was the most favorable acceptor for the reverse synthesis of NDP-Glc in k cat/Km. GDP and UDP were less preferred, compared to ADP. In a batch reaction of 12 h, the molar yield of NDP-Glc per NDP used was decreased approximately in the order of ADP-Glc > GDP-Glc > cytidine 5′-diphosphate (CDP)-Glc or UDP-Glc. The overall productivity of the enzyme was largely improved in a gram scale for NDP-Glcs using repetitive batch reactions with enzyme recycling. Thus, it is suggested that TreT from P. horikoshii may be useful for the regeneration of NDP-Glc from NDP, especially for ADP-Glc from ADP, with trehalose as a glucose resource.

Original languageEnglish
Pages (from-to)128-134
Number of pages7
JournalProcess Biochemistry
Volume46
Issue number1
DOIs
Publication statusPublished - 2011 Jan 1

Fingerprint

Pyrococcus horikoshii
Diphosphates
Recycling
Nucleosides
Glucose
Adenosine Diphosphate
Enzymes
Trehalose
Guanosine
Adenosine
Uridine Diphosphate
Cytidine Diphosphate
Catalysis
trehalose synthase
Uridine
Productivity
Regeneration
Cats
Substrates

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

Cite this

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title = "Catalytic reversibility of Pyrococcus horikoshii trehalose synthase: Efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling",
abstract = "The trehalose synthase (TreT) from Pyrococcus horikoshii represented reversible catalysis in alternative synthesis of trehalose and nucleoside 5′-diphosphate-glucose (NDP-Glc), depending on the substrates involved. TreT from P. horikoshii had differential preferences on NDP-Glc as a donor for trehalose synthesis, in which guanosine 5′-diphosphate (GDP)-Glc was the most favored in terms of reaction specificity, kcat/Km. Uridine 5′-diphosphate (UDP)- and adenosine 5′-diphosphate (ADP)-Glcs were employed with less preferences. This enzyme reversely cleaved trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-Glcs. Although ADP-Glc was the least favorable donor, the counterpart, ADP, was the most favorable acceptor for the reverse synthesis of NDP-Glc in k cat/Km. GDP and UDP were less preferred, compared to ADP. In a batch reaction of 12 h, the molar yield of NDP-Glc per NDP used was decreased approximately in the order of ADP-Glc > GDP-Glc > cytidine 5′-diphosphate (CDP)-Glc or UDP-Glc. The overall productivity of the enzyme was largely improved in a gram scale for NDP-Glcs using repetitive batch reactions with enzyme recycling. Thus, it is suggested that TreT from P. horikoshii may be useful for the regeneration of NDP-Glc from NDP, especially for ADP-Glc from ADP, with trehalose as a glucose resource.",
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Catalytic reversibility of Pyrococcus horikoshii trehalose synthase : Efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling. / Ryu, Soo In; Kim, Jeong Eun; Kim, Eun Joo; Chung, Seung Kyung; Lee, Soo-Bok.

In: Process Biochemistry, Vol. 46, No. 1, 01.01.2011, p. 128-134.

Research output: Contribution to journalArticle

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AU - Kim, Jeong Eun

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