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Literature summary for 3.2.1.176 extracted from

  • Smith, M.A.; Rentmeister, A.; Snow, C.D.; Wu, T.; Farrow, M.F.; Mingardon, F.; Arnold, F.H.
    A diverse set of family 48 bacterial glycoside hydrolase cellulases created by structure-guided recombination (2012), FEBS J., 279, 4453-4465.
    View publication on PubMed

Application

Application Comment Organism
biotechnology recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera Thermoclostridium stercorarium
biotechnology recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Two of the most stabilizing blocks are predicted to be from the parent CelS at blocks located in the C-terminus of the catalytic domain, close to where the dockerin attaches. Two of the highly stable chimeras also hydrolyze more cellulose than the most active parental enzyme Acetivibrio thermocellus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Acetivibrio thermocellus
expression in Escherichia coli Thermoclostridium stercorarium

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus A3DH67
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Acetivibrio thermocellus DSM 1237 A3DH67
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Thermoclostridium stercorarium P50900
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Thermoclostridium stercorarium DSM 8532 P50900
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-

Synonyms

Synonyms Comment Organism
celS
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Acetivibrio thermocellus
CelY
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Thermoclostridium stercorarium