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Essential role of the family-22 carbohydrate-binding modules for β-1,3-1,4-glucanase activity of Clostridium stercorarium Xyn10B
- Source :
- FEBS Letters; Mar2004, Vol. 561 Issue 1-3, p155, 4p
- Publication Year :
- 2004
-
Abstract
- Clostridium stercorarium Xyn10B is a modular enzyme comprising two family-22 carbohydrate-binding modules (CBMs), a family-10 catalytic module of glycoside hydrolases, a family-9 CBM, and two S-layer homologous modules consecutively from the N-terminus. To investigate the role of the family-22 CBMs, truncated proteins were constructed: a recombinant catalytic module polypeptide (rCD), a CBM polypeptide composed of two family-22 CBMs (rCBM) and a polypeptide composed of the family-22 CBMs and the catalytic module (rCBM-CD). We found that rCBM-CD was highly active toward β-1,3-1,4-glucan; however, rCD was negligibly active toward the same substrate. The V<subscript>max</subscript>/K<subscript>m</subscript> value of rCBM-CD for β-1,3-1,4-glucan was 7.8 times larger than that for oat-spelt xylan, indicating that rCBM-CD should be specified as a β-1,3-1,4-glucanase rather than a xylanase despite the fact that family-10 catalytic modules are well-known xylanase modules. These results indicate that the family-22 CBMs in rCBM-CD are essential for hydrolysis of β-1,3-1,4-glucan. [Copyright &y& Elsevier]
- Subjects :
- GLYCOSIDASES
GLUCAN synthase
CARRIER proteins
ENZYME kinetics
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 561
- Issue :
- 1-3
- Database :
- Complementary Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 12435483
- Full Text :
- https://doi.org/10.1016/S0014-5793(04)00160-7