Family 6 carbohydrate-binding modules display multiple β1,3-linked glucan-specific binding interfaces
نویسندگان
چکیده
منابع مشابه
Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.
Enzymes that hydrolyze complex carbohydrates play important roles in numerous biological processes that result in the maintenance of marine and terrestrial life. These enzymes often contain noncatalytic carbohydrate binding modules (CBMs) that have important substrate-targeting functions. In general, there is a tight correlation between the ligands recognized by bacterial CBMs and the substrate...
متن کاملFunctional studies and engineering of family 1 carbohydrate-binding modules
The family 1 cellulose-binding modules (CBM1) form a group of small, stable carbohydratebinding proteins. These modules are essential for fungal cellulose degradation. This thesis describes both functional studies of the CBM1s as well as protein engineering of the modules for several objectives. The characteristics and specificity of CBM1s from the Trichoderma reesei Cel7A and Cel6A, along with...
متن کاملIdentification and glucan-binding properties of a new carbohydrate-binding module family.
The C-terminal 191-residue module of Cel5A from the alkalophilic Bacillus sp. 1139 comprises a carbohydrate-binding module (CBM) belonging to a previously unidentified family that we have classified as CBM family 28. This example, called CBM28, bound specifically to cello-oligosaccharides and mixed beta-(1,3)(1,4)-glucans (barley beta-glucan) with association constants of approximately (1-4)x10...
متن کاملAffinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules
BACKGROUND Molecular evolution of carbohydrate binding modules (CBM) is a new approach for the generation of glycan-specific molecular probes. To date, the possibility of performing affinity maturation on CBM has not been investigated. In this study we show that binding characteristics such as affinity can be improved for CBM generated from the CBM4-2 scaffold by using random mutagenesis in com...
متن کاملThe binding pattern of two carbohydrate-binding modules of laminarinase Lam16A from Thermotoga neapolitana: differences in beta-glucan binding within family CBM4.
Carbohydrate-binding modules (CBMs) are often part of the complex hydrolytic extracellular enzymes from bacteria and may modulate their catalytic activity. The thermostable catalytic domain of laminarinase Lam16A from Thermotoga neapolitana (glycosyl hydrolase family 16) is flanked by two CBMs, 148 and 161 aa long. They share a sequence identity of 30%, are homologous to family CBM4 and are thu...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 2009
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.2009.01764.x