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Literature summary for 3.1.1.74 extracted from

  • Silva, C.; Da, S.; Silva, N.; Matama, T.; Araujo, R.; Martins, M.; Chen, S.; Chen, J.; Wu, J.; Casal, M.; Cavaco-Paulo, A.
    Engineered Thermobifida fusca cutinase with increased activity on polyester substrates (2011), Biotechnol. J., 6, 1230-1239.
    View publication on PubMed

Application

Application Comment Organism
synthesis application of enginered mutant T101A/Q132A/I218A in synthetic fiber biotransformation Thermobifida fusca

Protein Variants

Protein Variants Comment Organism
I218A engineering by site-directed mutagenesis modifying the active site, the mutant cutinase shows increased activity on polyester substrates. Mutation I218A creates space, activity on poly(ethylene terephthalate) is increased compared to the wild-type enzyme, with considerably higher hydrolysis efficiency Thermobifida fusca
T101A/Q132A engineering by site-directed mutagenesis modifying the active site, the mutant cutinase shows increased activity on polyester substrates. The double mutation Q132A/T101A both creates space and increases hydrophobicity. The activity of the double mutant on the soluble substrate p-nitrophenyl butyrate increased 2fold compared to wild-type cutinase, while on poly(ethylene terephthalate) the double mutant exhibits considerably higher hydrolysis efficiency Thermobifida fusca

Organism

Organism UniProt Comment Textmining
Thermobifida fusca
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-
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Synonyms

Synonyms Comment Organism
Tfu_0883
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Thermobifida fusca