Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


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
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ramsay, A. G.
Right arrow Articles by Flint, H. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ramsay, A. G.
Right arrow Articles by Flint, H. J.
Agricola
Right arrow Articles by Ramsay, A. G.
Right arrow Articles by Flint, H. J.
Microbiology 152 (2006), 3281-3290; DOI  10.1099/mic.0.29233-0
© 2006 Society for General Microbiology

Cell-associated {alpha}-amylases of butyrate-producing Firmicute bacteria from the human colon

Alan G. Ramsay{dagger}, Karen P. Scott, Jenny C. Martin, Marco T. Rincon and Harry J. Flint

Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK

Correspondence
Karen P. Scott
k.scott{at}rri.sari.ac.uk

Selected butyrate-producing bacteria from the human colon that are related to Roseburia spp. and Butyrivibrio fibrisolvens showed a good ability to utilize a variety of starches for growth when compared with the Gram-negative amylolytic anaerobe Bacteroides thetaiotaomicron. A major cell-associated amylase of high molecular mass (140–210 kDa) was detected in each strain by SDS-PAGE zymogram analysis, and genes corresponding to these enzymes were analysed for two representative strains. Amy13B from But. fibrisolvens 16/4 is a multi-domain enzyme of 144.6 kDa that includes a family 13 glycoside hydrolase domain, and duplicated family 26 carbohydrate-binding modules. Amy13A (182.4 kDa), from Roseburia inulinivorans A2-194, also includes a family 13 domain, which is preceded by two repeat units of ~116 aa rich in aromatic residues, an isoamylase N-terminal domain, a pullulanase-associated domain, and an additional unidentified domain. Both Amy13A and Amy13B have N-terminal signal peptides and C-terminal cell-wall sorting signals, including a modified LPXTG motif similar to that involved in interactions with the cell surface in other Gram-positive bacteria, a hydrophobic transmembrane segment, and a basic C terminus. The overexpressed family 13 domains showed an absolute requirement for Mg2+ or Ca2+ for activity, and functioned as 1,4-{alpha}-glucanohydrolases ({alpha}-amylases; EC 3.2.1.1). These major starch-degrading enzymes thus appear to be anchored to the cell wall in this important group of human gut bacteria.


Abbreviations: CBM, carbohydrate-binding module; HA, high-amylose; SP, signal peptide

The GenBank/EMBL/DDBJ accession numbers for the nucleotide sequences encoding the {alpha}-amylases of Butyrivibrio fibrisolvens and Roseburia inulinivorans are AJ578026 and AM055811, respectively.

{dagger}Present address: Centre for Tumour Biology, Institute of Cancer and CR-UK Clinical Centre, Bart's and The London Queen Mary's School of Medicine and Dentistry, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.




This article has been cited by other articles:


Home page
Appl. Environ. Microbiol.Home page
K. P. Scott, J. C. Martin, J. Mrazek, and H. J. Flint
Transfer of Conjugative Elements from Rumen and Human Firmicutes Bacteria to Roseburia inulinivorans
Appl. Envir. Microbiol., June 15, 2008; 74(12): 3915 - 3917.
[Abstract] [Full Text] [PDF]


Home page
Clin. Microbiol. Rev.Home page
H. M. Wexler
Bacteroides: the Good, the Bad, and the Nitty-Gritty
Clin. Microbiol. Rev., October 1, 2007; 20(4): 593 - 621.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
S. H. Duncan, A. Belenguer, G. Holtrop, A. M. Johnstone, H. J. Flint, and G. E. Lobley
Reduced Dietary Intake of Carbohydrates by Obese Subjects Results in Decreased Concentrations of Butyrate and Butyrate-Producing Bacteria in Feces
Appl. Envir. Microbiol., February 15, 2007; 73(4): 1073 - 1078.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2006 Society for General Microbiology.