Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The active site of a carbohydrate esterase displays divergent catalytic and noncatalytic binding functions.
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The CE2 domain (CtCE2) displays dual function with acetylxylan esterase/glucomannan deacetylase activity and cellulose-binding function, uniquely mediated through the same active site region.
"the CtCE2 domain displays divergent catalytic esterase and noncatalytic carbohydrate binding functions"
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CtCE2 binds cellooligosaccharides with high affinity.
"Isothermal titration calorimetry (ITC) revealed that CtCE2 binds to cellooligosaccharides with a K"
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The enzyme shows strong preference for glucomannan over xylan.
"Based on their catalytic efficiencies, CtCE2 and CjCE2B exhibit a significant preference for acetylated glucomannan over xylan"
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Cellulose binding inhibits esterase activity, demonstrating the overlap of catalytic and binding functions.
"cellohexaose and beta-glucan binding inhibit the esterase activity of the wild-type CtCE2 enzyme"
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The type I dockerin domain mediates incorporation into the cellulosome.
"The enzyme also contains a type I dockerin module that, by binding to cohesin modules in the scaffoldin protein, incorporates CtCel5C-CE2 into the multienzyme plant cell-wall-degrading complex known as the cellulosome"
Conserved reiterated domains in Clostridium thermocellum endoglucanases are not essential for catalytic activity.
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Original characterization of CelE as an endo-beta-1,4-glucanase with xylan-hydrolysing activity.
"The complete nucleotide sequence of the Clostridium thermocellum celE gene, coding for an endo-beta-1,4-glucanase (endoglucanase E; EGE) with xylan-hydrolysing activity has been determined"
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Identified the structural gene and confirmed N-terminal sequence of the purified protein.
"The nucleotide sequence obtained has been confirmed by comparing the predicted amino acid sequence with that derived by N-terminal amino acid sequencing of the purified protein"
The non-catalytic C-terminal region of endoglucanase E from Clostridium thermocellum contains a cellulose-binding domain.
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Demonstrated endoglucanase activity against CMC and barley beta-glucan.
"Mature endoglucanase E (EGE) from Clostridium thermocellum consists of 780 amino acid residues and has an Mr of 84,016. The N-terminal 334 amino acids comprise a functional catalytic domain"
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Identified the C-terminal cellulose-binding function.
"It is concluded that EGE contains a cellulose-binding domain, located between residues 432 and 671, that is distinct from the active site"