This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nagy, T. Articles by Gilbert, H. J. Search for Related Content PubMed PubMed Citation Articles by Nagy, T. Articles by Gilbert, H. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2002, p. 4925-4929, Vol. 184, No. 17
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.17.4925-4929.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Membrane-Bound -Glucuronidase from Pseudomonas cellulosa Hydrolyzes 4-O-Methyl-D-Glucuronoxylooligosaccharides but Not 4-O-Methyl-D-Glucuronoxylan

Department of Biological and Nutritional Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne NE1 7RU,¹ School of Sciences, University of Sunderland, Sunderland SR1 3SD, United Kingdom,³ CIISA-Faculdade de Medicina Veterinaria, 1199 Lisbon Codex, Portugal²

Received 1 April 2002/ Accepted 27 May 2002

The microbial degradation of xylan is a key biological process. Hardwood 4-O-methyl-D-glucuronoxylans are extensively decorated with 4-O-methyl-D-glucuronic acid, which is cleaved from the polysaccharides by -glucuronidases. In this report we describe the primary structures of the -glucuronidase from Cellvibrio mixtus (C. mixtus GlcA67A) and the -glucuronidase from Pseudomonas cellulosa (P. cellulosa GlcA67A) and characterize P. cellulosa GlcA67A. The primary structures of C. mixtus GlcA67A and P. cellulosa GlcA67A, which are 76% identical, exhibit similarities with -glucuronidases in glycoside hydrolase family 67. The membrane-associated pseudomonad -glucuronidase released 4-O-methyl-D-glucuronic acid from 4-O-methyl-D-glucuronoxylooligosaccharides but not from 4-O-methyl-D-glucuronoxylan. We propose that the role of the glucuronidase, in combination with cell-associated xylanases, is to hydrolyze decorated xylooligosaccharides, generated by extracellular hemicellulases, to xylose and 4-O-methyl-D-glucuronic acid, enabling the pseudomonad to preferentially utilize the sugars derived from these polymers.

This article has been cited by other articles:

• DeBoy, R. T., Mongodin, E. F., Fouts, D. E., Tailford, L. E., Khouri, H., Emerson, J. B., Mohamoud, Y., Watkins, K., Henrissat, B., Gilbert, H. J., Nelson, K. E. (2008). Insights into Plant Cell Wall Degradation from the Genome Sequence of the Soil Bacterium Cellvibrio japonicus. J. Bacteriol. 190: 5455-5463 [Abstract] [Full Text]  
• Shulami, S., Zaide, G., Zolotnitsky, G., Langut, Y., Feld, G., Sonenshein, A. L., Shoham, Y. (2007). A Two-Component System Regulates the Expression of an ABC Transporter for Xylo-Oligosaccharides in Geobacillus stearothermophilus. Appl. Environ. Microbiol. 73: 874-884 [Abstract] [Full Text]  
• St. John, F. J., Rice, J. D., Preston, J. F. (2006). Characterization of XynC from Bacillus subtilis subsp. subtilis Strain 168 and Analysis of Its Role in Depolymerization of Glucuronoxylan. J. Bacteriol. 188: 8617-8626 [Abstract] [Full Text]  
• StJohn, F. J., Rice, J. D., Preston, J. F. (2006). Paenibacillus sp. Strain JDR-2 and XynA1: a Novel System for Methylglucuronoxylan Utilization. Appl. Environ. Microbiol. 72: 1496-1506 [Abstract] [Full Text]  
• Shallom, D., Golan, G., Shoham, G., Shoham, Y. (2004). Effect of Dimer Dissociation on Activity and Thermostability of the {alpha}-Glucuronidase from Geobacillus stearothermophilus: Dissecting the Different Oligomeric Forms of Family 67 Glycoside Hydrolases. J. Bacteriol. 186: 6928-6937 [Abstract] [Full Text]  
• Adelsberger, H., Hertel, C., Glawischnig, E., Zverlov, V. V., Schwarz, W. H. (2004). Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes. Microbiology 150: 2257-2266 [Abstract] [Full Text]  
• Dias, F. M. V., Vincent, F., Pell, G., Prates, J. A. M., Centeno, M. S. J., Tailford, L. E., Ferreira, L. M. A., Fontes, C. M. G. A., Davies, G. J., Gilbert, H. J. (2004). Insights into the Molecular Determinants of Substrate Specificity in Glycoside Hydrolase Family 5 Revealed by the Crystal Structure and Kinetics of Cellvibrio mixtus Mannosidase 5A. J. Biol. Chem. 279: 25517-25526 [Abstract] [Full Text]  
• Pell, G., Szabo, L., Charnock, S. J., Xie, H., Gloster, T. M., Davies, G. J., Gilbert, H. J. (2004). Structural and Biochemical Analysis of Cellvibrio japonicus Xylanase 10C: HOW VARIATION IN SUBSTRATE-BINDING CLEFT INFLUENCES THE CATALYTIC PROFILE OF FAMILY GH-10 XYLANASES. J. Biol. Chem. 279: 11777-11788 [Abstract] [Full Text]  
• Pell, G., Taylor, E. J., Gloster, T. M., Turkenburg, J. P., Fontes, C. M. G. A., Ferreira, L. M. A., Nagy, T., Clark, S. J., Davies, G. J., Gilbert, H. J. (2004). The Mechanisms by Which Family 10 Glycoside Hydrolases Bind Decorated Substrates. J. Biol. Chem. 279: 9597-9605 [Abstract] [Full Text]  
• Nagy, T., Nurizzo, D., Davies, G. J., Biely, P., Lakey, J. H., Bolam, D. N., Gilbert, H. J. (2003). The {alpha}-Glucuronidase, GlcA67A, of Cellvibrio japonicus Utilizes the Carboxylate and Methyl Groups of Aldobiouronic Acid as Important Substrate Recognition Determinants. J. Biol. Chem. 278: 20286-20292 [Abstract] [Full Text]  
• Charnock, S. J., Brown, I. E., Turkenburg, J. P., Black, G. W., Davies, G. J. (2002). Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases. Proc. Natl. Acad. Sci. USA 99: 12067-12072 [Abstract] [Full Text]