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

Anat Ezer; Erez Matalon; Sadanari Jindou; Ilya Borovok; Nof Atamna; Zhongtang Yu; Mark Morrison; Edward A. Bayer; Raphael Lamed

doi:10.1128/JB.00609-08

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

Anat Ezer, Erez Matalon, Sadanari Jindou, Ilya Borovok, Nof Atamna, Zhongtang Yu, Mark Morrison, Edward A. Bayer, Raphael Lamed

Biotechnology

Research output: Contribution to journal › Article › peer-review

51 Scopus citations

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.

Original language	English
Pages (from-to)	8220-8222
Number of pages	3
Journal	Journal of Bacteriology
Volume	190
Issue number	24
DOIs	https://doi.org/10.1128/JB.00609-08
State	Published - Dec 2008

Access to Document

10.1128/JB.00609-08

Cite this

@article{c0dd9f98accf4520b0fb568e13439faf,

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

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.",

author = "Anat Ezer and Erez Matalon and Sadanari Jindou and Ilya Borovok and Nof Atamna and Zhongtang Yu and Mark Morrison and Bayer, {Edward A.} and Raphael Lamed",

year = "2008",

month = dec,

doi = "10.1128/JB.00609-08",

language = "אנגלית",

volume = "190",

pages = "8220--8222",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

number = "24",

}

TY - JOUR

T1 - Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus

AU - Ezer, Anat

AU - Matalon, Erez

AU - Jindou, Sadanari

AU - Borovok, Ilya

AU - Atamna, Nof

AU - Yu, Zhongtang

AU - Morrison, Mark

AU - Bayer, Edward A.

AU - Lamed, Raphael

PY - 2008/12

Y1 - 2008/12

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=57349113816&partnerID=8YFLogxK

U2 - 10.1128/JB.00609-08

DO - 10.1128/JB.00609-08

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:57349113816

SN - 0021-9193

VL - 190

SP - 8220

EP - 8222

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 24

ER -

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

Abstract

Access to Document

Other files and links

Fingerprint

Cite this