Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus

Ezer, Anat, Matalon, Erez, Jindou, Sadanari, Borovok, Ilya, Atamna, Nof, Zhongtang, Yu, Morrison, Mark, Bayer, Edward A. and Lamed, Raphael (2008) Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus. Journal of Bacteriology, 190 24: 8220-8222. doi:10.1128/JB.00609-08

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Author Ezer, Anat
Matalon, Erez
Jindou, Sadanari
Borovok, Ilya
Atamna, Nof
Zhongtang, Yu
Morrison, Mark
Bayer, Edward A.
Lamed, Raphael
Title Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 1098-5530
0021-9193
Publication date 2008-12
Sub-type Article (original research)
DOI 10.1128/JB.00609-08
Open Access Status File (Publisher version)
Volume 190
Issue 24
Start page 8220
End page 8222
Total pages 3
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Abstract The rumen bacterium Ruminococcus albus binds to and degrades crystalline cellulosic substrates via a unique cellulose degradation system. A unique family of carbohydrate-binding modules (CBM37), located at the C terminus of different glycoside hydrolases, appears to be responsible both for anchoring these enzymes to the bacterial cell surface and for substrate binding.
Keyword Ruminococcus albus
Rumen bacterium
Cellulose degradation
Carbohydrate binding molecules
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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Created: Mon, 04 Jan 2010, 14:20:08 EST by Elissa Saffery on behalf of Faculty of Science