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

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, June 1999, p. 2598-2605, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Mannan-Degrading Enzymes from Cellulomonas fimi

Dominik Stoll, Henrik Stålbrand,dagger and R. Antony J. Warren*

Department of Microbiology and Immunology and The Protein Engineering Network of Centres of Excellence, The University of British Columbia, Vancouver, British Columbia, Canada

Received 15 December 1998/Accepted 22 February 1999

The genes man26a and man2A from Cellulomonas fimi encode mannanase 26A (Man26A) and beta -mannosidase 2A (Man2A), respectively. Mature Man26A is a secreted, modular protein of 951 amino acids, comprising a catalytic module in family 26 of glycosyl hydrolases, an S-layer homology module, and two modules of unknown function. Exposure of Man26A produced by Escherichia coli to C. fimi protease generates active fragments of the enzyme that correspond to polypeptides with mannanase activity produced by C. fimi during growth on mannans, indicating that it may be the only mannanase produced by the organism. A significant fraction of the Man26A produced by C. fimi remains cell associated. Man2A is an intracellular enzyme comprising a catalytic module in a subfamily of family 2 of the glycosyl hydrolases that at present contains only mammalian beta -mannosidases.


* Corresponding author. Mailing address: Department of Microbiology and Immunology, University of British Columbia, 300-6174 University Blvd., Vancouver, BC, Canada V6T 1Z3. Phone: (604) 822-2376. Fax: (604) 822-6041. E-mail: rajw{at}unixg.ubc.ca.

dagger Present address: Department of Biochemistry, University of Lund, Lund, Sweden.


Applied and Environmental Microbiology, June 1999, p. 2598-2605, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Cartmell, A., Topakas, E., Ducros, V. M-A., Suits, M. D. L., Davies, G. J., Gilbert, H. J. (2008). The Cellvibrio japonicus Mannanase CjMan26C Displays a Unique exo-Mode of Action That Is Conferred by Subtle Changes to the Distal Region of the Active Site. J. Biol. Chem. 283: 34403-34413 [Abstract] [Full Text]  
  • Sasaki, A., Ishimizu, T., Hase, S. (2005). Substrate Specificity and Molecular Cloning of the Lily Endo-{beta}-Mannosidase Acting on N-Glycan. J Biochem 137: 87-93 [Abstract] [Full Text]  
  • Ishimizu, T., Sasaki, A., Okutani, S., Maeda, M., Yamagishi, M., Hase, S. (2004). Endo-{beta}-mannosidase, a Plant Enzyme Acting on N-Glycan: PURIFICATION, MOLECULAR CLONING, AND CHARACTERIZATION. J. Biol. Chem. 279: 38555-38562 [Abstract] [Full Text]  
  • Beki, E., Nagy, I., Vanderleyden, J., Jager, S., Kiss, L., Fulop, L., Hornok, L., Kukolya, J. (2003). Cloning and Heterologous Expression of a {beta}-D-Mannosidase (EC 3.2.1.25)-Encoding Gene from Thermobifida fusca TM51. Appl. Environ. Microbiol. 69: 1944-1952 [Abstract] [Full Text]  
  • Hogg, D., Woo, E.-J., Bolam, D. N., McKie, V. A., Gilbert, H. J., Pickersgill, R. W. (2001). Crystal Structure of Mannanase 26A from Pseudomonas cellulosa and Analysis of Residues Involved in Substrate Binding. J. Biol. Chem. 276: 31186-31192 [Abstract] [Full Text]