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Literature summary for 3.2.1.4 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 Ruminiclostridium cellulolyticum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Ruminiclostridium cellulolyticum

Organism

Organism UniProt Comment Textmining
Ruminiclostridium cellulolyticum P37698
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Ruminiclostridium cellulolyticum DSM 5812 P37698
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Synonyms

Synonyms Comment Organism
CelF
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Ruminiclostridium cellulolyticum