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In molecular biology, the CHB HEX N-terminal domain represents the N-terminal domain in and beta-hexosaminidases. Chitobiases degrade chitin, which forms the exoskeleton in insects and crustaceans, and which is one of the most abundant polysaccharides on earth. Beta-hexosaminidases are composed of either a HexA/HexB heterodimer or a HexB homodimer, and can hydrolyse diverse substrates, including GM(2)-gangliosides; mutations in this enzyme are associated with Tay–Sachs disease. HexB is structurally similar to chitobiase, consisting of a beta sandwich structure; this structure is similar to that found in the cellulose-binding domain of cellulase from Cellulomonas fimi. This domain may function as a carbohydrate binding module.

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dbo:abstract
  • In molecular biology, the CHB HEX N-terminal domain represents the N-terminal domain in and beta-hexosaminidases. Chitobiases degrade chitin, which forms the exoskeleton in insects and crustaceans, and which is one of the most abundant polysaccharides on earth. Beta-hexosaminidases are composed of either a HexA/HexB heterodimer or a HexB homodimer, and can hydrolyse diverse substrates, including GM(2)-gangliosides; mutations in this enzyme are associated with Tay–Sachs disease. HexB is structurally similar to chitobiase, consisting of a beta sandwich structure; this structure is similar to that found in the cellulose-binding domain of cellulase from Cellulomonas fimi. This domain may function as a carbohydrate binding module. (en)
dbo:symbol
  • CHB_HEX
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  • 32251110 (xsd:integer)
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  • 2203 (xsd:nonNegativeInteger)
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  • 995826717 (xsd:integer)
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dbp:caption
  • 4.6656E7
dbp:interpro
  • IPR004866 (en)
dbp:name
  • CHB HEX N-terminal domain (en)
dbp:pfam
  • PF03173 (en)
dbp:pfamClan
  • CL0203 (en)
dbp:scop
  • 7.0
dbp:symbol
  • CHB_HEX (en)
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rdfs:comment
  • In molecular biology, the CHB HEX N-terminal domain represents the N-terminal domain in and beta-hexosaminidases. Chitobiases degrade chitin, which forms the exoskeleton in insects and crustaceans, and which is one of the most abundant polysaccharides on earth. Beta-hexosaminidases are composed of either a HexA/HexB heterodimer or a HexB homodimer, and can hydrolyse diverse substrates, including GM(2)-gangliosides; mutations in this enzyme are associated with Tay–Sachs disease. HexB is structurally similar to chitobiase, consisting of a beta sandwich structure; this structure is similar to that found in the cellulose-binding domain of cellulase from Cellulomonas fimi. This domain may function as a carbohydrate binding module. (en)
rdfs:label
  • CHB HEX N-terminal domain (en)
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