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Journal of Bacteriology, May 1999, p. 3284-3287, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Type II Pullulanase of Thermococcus hydrothermalis: Molecular Characterization of the Gene and Expression of the Catalytic Domain

Marta Erra-Pujada,1,2 Philippe Debeire,1 Francis Duchiron,2 and Michael J. O'Donohue1,*

Unité de Physicochimie et Biotechnologie des Polymères, Institut National de la Recherche Agronomique,1 and Laboratoire de Microbiologie Industrielle, Université de Reims Champagne-Ardenne,2 51687 Reims Cedex 02, France

Received 28 December 1998/Accepted 19 March 1999

The gene encoding a hyperthermostable type II pullulanase produced by Thermococcus hydrothermalis (Th-Apu) has been isolated. Analysis of a total of 5.2 kb of genomic DNA has revealed the presence of three open reading frames, one of which (apuA) encodes the pullulanase. This enzyme is composed of 1,339 amino acid residues and exhibits a multidomain structure. In addition to a typical N-terminal signal peptide, Th-Apu possesses a catalytic domain, a domain bearing S-layer homology-like motifs, a Thr-rich region, and a potential C-terminal transmembrane domain. The presence of these noncatalytic domains suggests that Th-Apu may be anchored to the cell surface and be O glycosylated.

* Corresponding author. Mailing address: Unité de Physicochimie et Biotechnologie des Polymères, Institut National de la Recherche Agronomique, Université de Reims Champagne-Ardenne, Bât. 18, Moulin de la Housse, BP 1039, 51687 Reims Cedex 02, France. Phone: (33) 3 26 91 32 24. Fax: (33) 3 26 91 38 87. E-mail: odonohue{at}lille.inra.fr.

Journal of Bacteriology, May 1999, p. 3284-3287, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.




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