Difference between revisions of "Part:BBa K4275041"
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Strong promoter and terminator are used for high production.The protein produced has the ability to interact with 2 enzymatic subunits that are fused with a type I dockerin because the primary scaffoldin contains 2 type I cohesin domain. The cohesin-dockerin interaction fixes the subunits onto the primary scaffold allowing the enzymes to work synergetically to perform a cascade of catalytical reactions. One CBM ensures the cellulose or PET in the surrounding are attracted to the domains and allows them to be digested. | Strong promoter and terminator are used for high production.The protein produced has the ability to interact with 2 enzymatic subunits that are fused with a type I dockerin because the primary scaffoldin contains 2 type I cohesin domain. The cohesin-dockerin interaction fixes the subunits onto the primary scaffold allowing the enzymes to work synergetically to perform a cascade of catalytical reactions. One CBM ensures the cellulose or PET in the surrounding are attracted to the domains and allows them to be digested. | ||
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| + | ===Usage and Biology=== | ||
The protein scaffold of the mimic primary scaffoldin component contains 2 type I cohesin domain that interacts with the type I dockerin domain fused on other fusion protein to fix them onto the scaffold as a complex, the CBM domain on the protein attracts PET and cellulose in the surrounding, generating close proximity between the fixed enzyme on the scaffold and the substrate in the case of cellulose and PET degradation, for the catalytical reactions to happen faster. The primary scaffold can also be assembled to the secondary scaffold as it contains a type II dockerin domain to construct larger cellulosome-like complexes. And the paired strong promoter and terminator grants efficient production of the protein. | The protein scaffold of the mimic primary scaffoldin component contains 2 type I cohesin domain that interacts with the type I dockerin domain fused on other fusion protein to fix them onto the scaffold as a complex, the CBM domain on the protein attracts PET and cellulose in the surrounding, generating close proximity between the fixed enzyme on the scaffold and the substrate in the case of cellulose and PET degradation, for the catalytical reactions to happen faster. The primary scaffold can also be assembled to the secondary scaffold as it contains a type II dockerin domain to construct larger cellulosome-like complexes. And the paired strong promoter and terminator grants efficient production of the protein. | ||
| − | + | ===Sequence and Features=== | |
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<partinfo>BBa_K4275041 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4275041 SequenceAndFeatures</partinfo> | ||
Revision as of 07:53, 12 October 2022
pT7-RBS-CipA1B2C-tT7
Strong promoter and terminator are used for high production.The protein produced has the ability to interact with 2 enzymatic subunits that are fused with a type I dockerin because the primary scaffoldin contains 2 type I cohesin domain. The cohesin-dockerin interaction fixes the subunits onto the primary scaffold allowing the enzymes to work synergetically to perform a cascade of catalytical reactions. One CBM ensures the cellulose or PET in the surrounding are attracted to the domains and allows them to be digested.
Usage and Biology
The protein scaffold of the mimic primary scaffoldin component contains 2 type I cohesin domain that interacts with the type I dockerin domain fused on other fusion protein to fix them onto the scaffold as a complex, the CBM domain on the protein attracts PET and cellulose in the surrounding, generating close proximity between the fixed enzyme on the scaffold and the substrate in the case of cellulose and PET degradation, for the catalytical reactions to happen faster. The primary scaffold can also be assembled to the secondary scaffold as it contains a type II dockerin domain to construct larger cellulosome-like complexes. And the paired strong promoter and terminator grants efficient production of the protein.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 2073
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 354
Illegal XhoI site found at 1277 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 583
Illegal AgeI site found at 365
Illegal AgeI site found at 709
Illegal AgeI site found at 908
Illegal AgeI site found at 1579 - 1000COMPATIBLE WITH RFC[1000]