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Research article

A novel α-glucosidase from the acidophilic archaeon Ferroplasma acidiphilum strain Y with high transglycosylation activity and an unusual catalytic nucleophile

Manuel Ferrer, Olga V. Golyshina, Francisco J. Plou, Kenneth N. Timmis, Peter N. Golyshin
Biochemical Journal Oct 10, 2005, 391 (2) 269-276; DOI: 10.1042/BJ20050346
Manuel Ferrer
Department of Microbiology, German Research Centre for Biotechnology (GFB), Mascheroder Weg 1, 38124 Braunschweig, GermanyDepartment of Biocatalysis, Institute of Catalysis, CSIC (Consejo Superior de Investigaciones Científicas), Cantoblanco, 28049 Madrid, Spain
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  • For correspondence: mferrer@icp.csic.es
Olga V. Golyshina
Department of Microbiology, German Research Centre for Biotechnology (GFB), Mascheroder Weg 1, 38124 Braunschweig, Germany
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Francisco J. Plou
Department of Biocatalysis, Institute of Catalysis, CSIC (Consejo Superior de Investigaciones Científicas), Cantoblanco, 28049 Madrid, Spain
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Kenneth N. Timmis
Department of Microbiology, German Research Centre for Biotechnology (GFB), Mascheroder Weg 1, 38124 Braunschweig, GermanyInstitute of Microbiology, Technical University of Braunschweig, Biozentrum, Spielmannstr. 7, 38106 Braunschweig, Germany
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Peter N. Golyshin
Department of Microbiology, German Research Centre for Biotechnology (GFB), Mascheroder Weg 1, 38124 Braunschweig, GermanyInstitute of Microbiology, Technical University of Braunschweig, Biozentrum, Spielmannstr. 7, 38106 Braunschweig, Germany
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Abstract

Ferroplasma acidiphilum strain Y (DSM 12658), a ferrous iron-oxidizing, acidophilic and mesophilic archaeon, was found to produce a membrane-bound α-glucosidase (αGluFa) showing no significant similarity to any of the known glycoside hydrolases classified in different families and having an unusual catalytic site consisting of a threonine and a histidine residue. The highest α-glucosidase activity was found at low pH, 2.4–3.5, and the substrate preference order was: sucrose>maltose>maltotriose ≫maltotetraose≫malto-oligosaccharides from maltopentaose to maltoheptaose⋙soluble starch (kcat/Km was 293.0, 197.0, 18.8, 0.3 and 0.02 s−1·mM−1 respectively). The enzyme was able to transfer glucosyl groups from maltose as donor, to produce exclusively maltotriose (up to 300 g/l). Chemical modification and electrospray ionization MS analysis of 5-fluoro-α-D-glucopyranosyl-enzyme derivatives, coupled with site-directed mutagenesis, strongly suggested that the putative catalytic nucleophile in this enzyme is Thr212. Iron was found to be essential for enzyme activity and integrity, and His390 was shown to be essential for iron binding. These results suggest that the metalloenzyme αGluFa is a new member of the glycosyl hydrolase family that uses a novel mechanism for sugar glycosylation and/or transglycosylation.

  • α-glucosidase
  • catalytic nucleophile
  • Ferroplasma acidiphilum
  • glucosyl transferase
  • glycosyl hydrolase
  • transglycosylation

Abbreviations: iPr2P-F, di-isopropyl fluorophosphate (‘DFP’); EDC, 1-ethyl-3-[3-(dimethylamino)propyl]carbodi-imide; ESI-MS, electrospray ionization MS; 5FαGlcF, 5-fluoro-α-D-glucopyranosyl fluoride; GH, glycoside hydrolase; ICP-MS, inductively coupled plasma MS; IPTG, isopropyl β-D-thiogalactoside; LB, Luria–Bertani; PCMPS, p-chloromercuriphenylsulphonic acid; TNM, tetranitromethane; αGluFa, α-glucosidase from Ferroplasma acidiphilum strain YT

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October 2005

Volume: 391 Issue: 2

Biochemical Journal: 391 (2)
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A novel α-glucosidase from the acidophilic archaeon Ferroplasma acidiphilum strain Y with high transglycosylation activity and an unusual catalytic nucleophile
Manuel Ferrer, Olga V. Golyshina, Francisco J. Plou, Kenneth N. Timmis, Peter N. Golyshin
Biochemical Journal Oct 2005, 391 (2) 269-276; DOI: 10.1042/BJ20050346
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A novel α-glucosidase from the acidophilic archaeon Ferroplasma acidiphilum strain Y with high transglycosylation activity and an unusual catalytic nucleophile
Manuel Ferrer, Olga V. Golyshina, Francisco J. Plou, Kenneth N. Timmis, Peter N. Golyshin
Biochemical Journal Oct 2005, 391 (2) 269-276; DOI: 10.1042/BJ20050346

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Keywords

α-glucosidase
catalytic nucleophile
Ferroplasma acidiphilum
glucosyl transferase
glycosyl hydrolase
transglycosylation

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