Cell Surface Enzyme Attachment Is Mediated by Family 37 Carbohydrate-Binding Modules, Unique to Ruminococcus albus | Zendy

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

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Cell Surface Enzyme Attachment Is Mediated by Family 37 Carbohydrate-Binding Modules, Unique to Ruminococcus albus

Author(s) -

Anat Ezer,

Erez Matalon,

Sadanari Jindou,

Ilya Borovok,

Nof Atamna,

Zhongtang Yu,

Mark Morrison,

Edward A. Bayer,

Raphael Lamed

Publication year - 2008

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.00609-08

Subject(s) - ruminococcus , biology , carbohydrate binding module , glycoside hydrolase , biochemistry , enzyme , cell wall , binding site , gut flora

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.

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