In:
FEBS Letters, Wiley, Vol. 561, No. 1-3 ( 2004-03-12), p. 155-158
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 max / K m 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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(04)00160-7
Language:
English
Publisher:
Wiley
Publication Date:
2004
detail.hit.zdb_id:
1460391-3
SSG:
12
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