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J. Biol. Chem., Vol. 275, Issue 29, 22082-22089, July 21, 2000
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From the We here report the first molecular
characterization of an The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ251975.
Identification and Molecular Characterization of the First
-Xylosidase from an Archaeon*
§,,,
,,¶¶
Institute of Protein Biochemistry and
Enzymology, Consiglio Nazionale delle Ricerche (CNR), 80125 Naples,
Italy, the ¶ Istituto per la Chimica di Molecole di Interesse
Biologico, CNR, 80072 Naples, Italy, the Istituto di
Farmacologia e Tossicologia, Seconda Universita' di Napoli, Centro
Ricerche Interdipartimentale Biomateriali (CRIB), 80138 Naples, Italy,
the ** Laboratory of Microbiology, Department of Biomolecular Sciences,
Wageningen University, NL-6703 CT Wageningen, The Netherlands, the
Institute for Marine Biosciences,
National Research Council of Canada, Halifax, Nova Scotia B3H 3Z1,
Canada, the §§ Department of Biology,
University of Ottawa, Ontario K1N 6N5, Canada, and the
¶¶ Dipartimento di Chimica Organica e Biologica,
Universita' di Napoli "Federico II," 80134 Naples, Italy
-xylosidase (XylS) from an Archaeon.
Sulfolobus solfataricus is able to grow at temperatures higher
than 80 °C on several carbohydrates at acidic pH. The isolated
xylS gene encodes a monomeric enzyme homologous to
-glucosidases, -xylosidases, glucoamylases and sucrase-isomaltases of the glycosyl hydrolase family 31. xylS belongs to a cluster of four genes in the S. solfataricus genome, including a 
-glycosidase, an hypothetical
membrane protein homologous to the major facilitator superfamily of
transporters, and an open reading frame of unknown function. The
-xylosidase was overexpressed in Escherichia coli
showing optimal activity at 90 °C and a half-life at this
temperature of 38 h. The purified enzyme follows a
retaining mechanism of substrate hydrolysis, showing high
hydrolytic activity on the disaccharide isoprimeverose and catalyzing
the release of xylose from xyloglucan oligosaccharides. Synergy is
observed in the concerted in vitro hydrolysis of xyloglucan
oligosaccharides by the -xylosidase and the -glycosidase from
S. solfataricus. The analysis of the total S. solfataricus RNA revealed that all the genes of the cluster are
actively transcribed and that xylS and orf3 genes are cotranscribed.
*
Supported by the European Union (contract BIO-4CT960270;
this is the National Research Council of Canada publication number 42323).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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