In molecular biology, a carbohydrate-binding module (CBM) is a protein domain found in carbohydrate-active enzymes (for example glycoside hydrolases). The majority of these domains have carbohydrate-binding activity. Some of these domains are found on cellulosomal scaffoldin proteins. CBMs were previously known as cellulose-binding domains.[1] CBMs are classified into numerous families, based on amino acid sequence similarity. There are currently (June 2011) 64 families of CBM in the CAZy database.[2]
Quick Facts CBM_1, Identifiers ...
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Quick Facts CBM_2, Identifiers ...
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Quick Facts CBM_3, Identifiers ...
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Quick Facts CBM_5/12, Identifiers ...
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Quick Facts CBM_6, Identifiers ...
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Quick Facts CBM_4/9, Identifiers ...
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Quick Facts CBM_10, Identifiers ...
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Quick Facts CBM_11, Identifiers ...
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Quick Facts CBM_14, Identifiers ...
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Quick Facts CBM_15, Identifiers ...
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Quick Facts CBM_17/28, Identifiers ...
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Quick Facts Chitin_bind_1 (CBM18), Identifiers ...
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Quick Facts CBM_19, Identifiers ...
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Quick Facts CBM_20, Identifiers ...
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Quick Facts CBM_21, Identifiers ...
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Quick Facts CBM_25, Identifiers ...
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Quick Facts CBM27, Identifiers ...
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Quick Facts Chitin_bind_3 (CBM33), Identifiers ...
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Quick Facts CBM_48, Identifiers ...
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Quick Facts CBM49, Identifiers ...
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CBMs of microbial glycoside hydrolases play a central role in the recycling of photosynthetically fixed carbon through their binding to specific plant structural polysaccharides.[3] CBMs can recognise both crystalline and amorphous cellulose forms.[4] CBMs are the most common non-catalytic modules associated with enzymes active in plant cell-wall hydrolysis. Many putative CBMs have been identified by amino acid sequence alignments but only a few representatives have been shown experimentally to have a carbohydrate-binding function.[5]