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Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum

Authors
  • Sakuraba, Haruhiko
  • Yokono, Kaori
  • Yoneda, Kazunari
  • Watanabe, Akira
  • Asada, Yasuhiko
  • Satomura, Takenori
  • Yabutani, Tomoki
  • Motonaka, Junko
  • Ohshima, Toshihisa
Type
Published Article
Journal
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Publication Date
Jan 01, 2010
Volume
502
Issue
2
Pages
81–88
Identifiers
DOI: 10.1016/j.abb.2010.08.002
Source
Elsevier
Keywords
License
Unknown

Abstract

We identified a gene encoding a soluble quinoprotein glucose dehydrogenase homologue in the hyperthermophilic archaeon Pyrobaculum aerophilum. The gene was overexpressed in Escherichia coli, after which its product was purified and characterized. The enzyme was extremely thermostable, and the activity of the pyrroloquinoline quinone (PQQ)-bound holoenzyme was not lost after incubation at 100 °C for 10 min. The crystal structure of the enzyme was determined in both the apoform and as the PQQ-bound holoenzyme. The overall fold of the P. aerophilum enzyme showed significant similarity to that of soluble quinoprotein aldose sugar dehydrogenase (Asd) from E. coli. However, clear topological differences were observed in the two long loops around the PQQ-binding sites of the two enzymes. Structural comparison revealed that the hyperthermostability of the P. aerophilum enzyme is likely attributable to the presence of an extensive aromatic pair network located around a β-sheet involving N- and C-terminal β-strands.

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