Evidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus
1998
Karlsson, E.N. | Bartonek-Roxa, E. | Holst, O.
The xynl encoded 5 domain xylanase from the thermophilic bacterium Rhodothermus marinus binds specifically to xylan, beta-glucan and amorphous but not crystalline cellulose. Our results show that the binding is mediated by the full length xylanase, but not by the catalytic domain only. Based on similarities concerning both predicted secondary structure and binding specificity found with one cellulose binding domain of CenC from Cellulomonas fimi, we suggest that the binding is mediated by the two N-terminally repeated domains.
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书目信息
FEMS microbiology letters
卷
168
期
1
页码
1
- 7
ISSN
0378-1097
其它主题
Protein sorting signals; Protein structure; Secondary; Bacteroidetes; Substrate specificity; Polyacrylamide gel; Rhodothermus marinus; Xylanases; Catalytic domain; Amino acid sequence; Protein binding; Xylan endo-1; 3-beta-xylosidase; Cellulomonas fimi; Xylosidases; Molecular sequence data
语言
英语
类型
Journal Article; Text
2024-02-27
MODS