Team:Exeter/Basic Parts
Basic Parts
Click into the table to be directed to the registry pages, documenting our basic parts and our results for each of them. For further information regarding the origins of these parts, click on the reference link for the original research papers.
| Part Number | Part Name | Reference | ||
|---|---|---|---|---|
| BBa_K3039000 | PETase R280A
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the R208A mutant of PETase, with an N-terminal His-tag. The His-tag was added to allow for conformation of expression and subsequent purification. This mutation has been reported in past papers to increase the activity of PETase. |
Seongjoon Joo, In Jin Cho, Hogyun Seo, Hyeoncheol Francis Son, Hye-Young Sagong, Tae Joo Shin, So Young Choi, Sang Yup Lee & Kyung-Jin Kim; Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation (2018) Nat. Commun. 9(382) | ||
| BBa_K3039001 | PETase T88A_S121E_D186H_R280A
Different mutations that have been reported in past papers to increase the activity of PETase have been combined into a novel mutant, in order to test if this would result in an overly active mutant. This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the novel mutant of PETase, with an N-terminal His-tag. The His-tag was added to allow for conformation of expression and subsequent purification. |
Hyeoncheol Francis Son, In Jin Cho, Seongjoon Joo, Hogyun Seo, Hye-Young Sagong, So Young Choi, Sang Yup Lee, Kyung-Jin Kim; Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation (2019) ACS Catal. 9(4), 3519-3526 | ||
| BBa_K3039002 | PETase T88A_S93M_S121E_W159F_D186H_R280A
Different mutations that have been reported in past papers to increase the activity of PETase have been combined into a novel mutant, in order to test if this would result in an overly active mutant. This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the novel mutant of PETase, with an N-terminal His-tag. The His-tag was added to allow for conformation of expression and subsequent purification. |
Hyeoncheol Francis Son, In Jin Cho, Seongjoon Joo, Hogyun Seo, Hye-Young Sagong, So Young Choi, Sang Yup Lee, Kyung-Jin Kim; Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation (2019) ACS Catal. 9(4), 3519-3526
Congcong Liua, Chao Shia, Sujie Zhua, Risheng Weia, Chang-Cheng Yin; Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis (2019) Biochem. Biophys. Res. Commun. 508(1), 289-294 |
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| BBa_K3039003 | PETase S121E_D186H_R280A
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the S121E_D186H_R280A mutant of PETase, with an N-terminal His-tag. The His-tag was added to allow for conformation of expression and subsequent purification. The mutations have been reported in the literature to increase the thermostability of PETase and is therefore an improvement of the previous registry part BBa_K2010000. |
Hyeoncheol Francis Son, In Jin Cho, Seongjoon Joo, Hogyun Seo, Hye-Young Sagong, So Young Choi, Sang Yup Lee, Kyung-Jin Kim; Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation (2019) ACS Catal. 9(4), 3519-3526 | ||
| BBa_K3039004 | MHETase W397A
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the W397A mutant MHETase, with an N-terminal His-tag. The His-tag was added to allow for conformation of expression and subsequent purification. This mutations have been reported in past papers to increase the activity of MHETase. |
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717) | ||
| BBa_K3039005 | BHETase 1
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the S416A_F424N mutant MHETase, with an N-terminal His-tag. The His-tag was added to allow for conformation of expression and subsequent purification. These mutations have been reported in past papers to give MHETase the ability to degrade BHET. |
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717) | ||
| BBa_K3039006 | BHETase 2
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the R411A_S419G_F424N mutant MHETase, with an N-terminal His-tag. The His-tag was added to allow for conformation of expression and subsequent purification. The wild type MHETase doesn’t show BHET degrading activity. These mutations have been reported in past papers to give MHETase the ability to degrade BHET. |
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717) | ||
| BBa_K3039007 | SP_lamB-PETase
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of wild type PETase with a lamB signal peptide and N-terminal His-tag. The lamB signal peptide has been used for extracellular production of the enzyme when modified E.coli is added to the filter system and the His-tag is attached to more easily identify the enzymes. |
Hogyun Seo, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim; Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli (2019) Biochem. Biophys. Res. Commun. 508(1), 250-255
Shosuke Yoshida, Kazumi Hiraga, Toshihiko Takehana, Ikuo Taniguchi, Hironao Yamaji, Yasuhito Maeda, Kiyotsuna Toyohara, Kenji Miyamoto, Yoshiharu Kimura, Kohei Oda; A bacterium that degrades and assimilates poly(ethylene terephthalate) (2016) Science. 351(6278), 1196-1199 |
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| BBa_K3039008 | SP_lamB-PETase R280A
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the R208A mutant of PETase with the lamB signal peptide and N-terminal His-tag. The lamB signal peptide has been used for extracellular production of the enzyme when modified E.coli is added to the filter system and the His-tag is attached to more easily identify the enzymes. This mutation has been reported in past papers to increase the activity of PETase. |
Seongjoon Joo, In Jin Cho, Hogyun Seo, Hyeoncheol Francis Son, Hye-Young Sagong, Tae Joo Shin, So Young Choi, Sang Yup Lee & Kyung-Jin Kim; Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation (2018) Nat. Commun. 9(382)
Hogyun Seo, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim; Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli (2019) Biochem. Biophys. Res. Commun. 508(1), 250-255 |
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| BBa_K3039009 | SP_lamB-PETase W159H_S238F
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the W159H_S238F mutant of PETase with a lamB signal peptide and N-terminal His-tag. The lamB signal peptide has been used for extracellular production of the enzyme when modified E.coli is added to the filter system and the His-tag is attached to more easily identify the enzymes. These mutations have been reported in past papers to increase the thermostability of PETase. |
Harry P. Austin, Mark D. Allen, Bryon S. Donohoe, Nicholas A. Rorrer, Fiona L. Kearns, Rodrigo L. Silveira, Benjamin C. Pollard, Graham Dominick, Ramona Duman, Kamel El Omari, Vitaliy Mykhaylyk, Armin Wagner, William E. Michener, Antonella Amore, Munir S. Skaf, Michael F. Crowley, Alan W. Thorne, Christopher W. Johnson, H. Lee Woodcock, John E. McGeehan, and Gregg T. Beckham; Characterization and engineering of a plastic-degrading aromatic polyesterase (2018) PNAS, 115 (19)
Hogyun Seo, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim; Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli (2019) Biochem. Biophys. Res. Commun. 508(1), 250-255 |
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| BBa_K3039010 | SP_lamB-PETase T88A_S93M_S121E_W159F_D186H_R280A
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the T88A_S93M_S121E_W159F_D186H_R280A mutant of PETase with a lamB signal peptide and N-terminal His-tag. The lamB signal peptide has been used for extracellular production of the enzyme when modified E.coli is added to the filter system and the His-tag is attached to more easily identify the enzymes. These mutations have been reported in past papers to increase the thermostability of PETase. |
Hyeoncheol Francis Son, In Jin Cho, Seongjoon Joo, Hogyun Seo, Hye-Young Sagong, So Young Choi, Sang Yup Lee, Kyung-Jin Kim; Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation (2019) ACS Catal. 9(4), 3519-3526
Congcong Liua, Chao Shia, Sujie Zhua, Risheng Weia, Chang-Cheng Yin; Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis (2019) Biochem. Biophys. Res. Commun. 508(1), 289-294 Hogyun Seo, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim; Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli (2019) Biochem. Biophys. Res. Commun. 508(1), 250-255 |
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| BBa_K3039011 | SP_malE-MHETase
This sequence is the Escherichia. coli K12 (E. coli K12) codon optimized DNA of wild type MHETase with the malE signal peptide and N-terminal His-tag. The malE signal peptide has been used for extracellular production of the enzyme when modified E.coli is added to the filter system and the His-tag is attached to more easily identify the enzymes. |
Hogyun Seo, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim; Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli (2019) Biochem. Biophys. Res. Commun. 508(1), 250-255
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717) |
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| BBa_K3039012 | SP_malE-MHETase W397A
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the W397A mutant MHETase with the malE signal peptide and N-terminal His-tag. The malE signal peptide has been used for extracellular production of the enzyme when modified E.coli is added to the filter system and the His-tag is attached to more easily identify the enzymes. This mutation has been reported in past papers to increase the activity of MHETase. |
Hogyun Seo, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim; Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli (2019) Biochem. Biophys. Res. Commun. 508(1), 250-255
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717) |
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| BBa_K3039013 | SP_malE-MHETase S416A_F424N
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the S416A_F424N mutant MHETase with the malE signal peptide and N-terminal His-tag. The malE signal peptide has been used for extracellular production of the enzyme when modified E.coli is added to the filter system and the His-tag is attached to more easily identify the enzymes. The wild type MHETase doesn’t show BHET degrading activity. These mutation have been reported in past papers to give MHETase the ability to degrade BHET. |
Hogyun Seo, Seongmin Kim, Hyeoncheol Francis Son, Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim; Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli (2019) Biochem. Biophys. Res. Commun. 508(1), 250-255
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717) |
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| BBa_K3039014 | SP_ompA-MHETase
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of wild type MHETase with the ompA signal peptide and N-terminal His-tag. The ompA signal peptide has been used to secrete the enzyme into the periplasmic domain of E.coli when modified E.coli is added to the filter system and the His tag was attached in order to more easily identify the enzymes. |
Shosuke Yoshida, Kazumi Hiraga, Toshihiko Takehana, Ikuo Taniguchi, Hironao Yamaji, Yasuhito Maeda, Kiyotsuna Toyohara, Kenji Miyamoto, Yoshiharu Kimura, Kohei Oda; A bacterium that degrades and assimilates poly(ethylene terephthalate) (2016) Science. 351(6278), 1196-1199
Bernhard Fischer, Barry Perry, Gareth Phillips, lan Sumner, Peter Goodenough; Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli (1993) Appl. Microbiol. Biotechnol. 39(570) |
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| BBa_K3039015 | SP_ompA-MHETase W397A
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the W397A mutant MHETase with the ompA signal peptide and N-terminal His-tag. The ompA signal peptide has been used to secrete the enzyme into the periplasmic domain of E.coli when modified E.coli is added to the filter system and the His tag was attached in order to more easily identify the enzymes. This mutation has been reported in past papers to increase the activity of MHETase. |
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717)
Bernhard Fischer, Barry Perry, Gareth Phillips, lan Sumner, Peter Goodenough; Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli (1993) Appl. Microbiol. Biotechnol. 39(570) |
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| BBa_K3039016 | SP_ompA-MHETase S416A_F424N
This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the S416A_F424N mutant MHETase with the ompA signal peptide and N-terminal His-tag. The ompA signal peptide has been used to secrete the enzyme into the periplasmic domain of E.coli when modified E.coli is added to the filter system and the His tag was attached in order to more easily identify the enzymes. The wild type MHETase doesn’t show BHET degrading activity. These mutation has been reported in past papers to give MHETase the ability to degrade BHET. |
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer & Gert Weber; Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate (2019) Nat. Commun. 10(1717)
Bernhard Fischer, Barry Perry, Gareth Phillips, lan Sumner, Peter Goodenough; Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli (1993) Appl. Microbiol. Biotechnol. 39(570) |
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| BBa_K3039017 | Ancestral PETase 1
This is the sequence of one of the four reconstructed ancestors of PETase with a His tag attached to it. The sequence has been obtained through the method of ancestral reconstruction. The His-tag was added to allow for conformation of expression and subsequent purification. |
S F Altschul, W Gish, W Miller, E W Myers, D J Lipman; Basic local alignment search tool (1990) J. Mol. Biol. 215, 403-410.
Keiko Watanabe, Takatoshi Ohkuri, Shinichi Yokobori, Akihiko Yamagishi; Designing Thermostable Proteins: Ancestral Mutants of 3-Isopropylmalate Dehydrogenase Designed by using a Phylogenetic Tree (2006) J. Mol. Biol. 355(4), 664-674 |
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| BBa_K3039018 | Ancestral PETase 2
This is the sequence of one of the four reconstructed ancestors of PETase with a His tag attached to it. The sequence has been obtained through the method of ancestral reconstruction. The His-tag was added to allow for conformation of expression and subsequent purification. |
S F Altschul, W Gish, W Miller, E W Myers, D J Lipman; Basic local alignment search tool (1990) J. Mol. Biol. 215, 403-410.
Keiko Watanabe, Takatoshi Ohkuri, Shinichi Yokobori, Akihiko Yamagishi; Designing Thermostable Proteins: Ancestral Mutants of 3-Isopropylmalate Dehydrogenase Designed by using a Phylogenetic Tree (2006) J. Mol. Biol. 355(4), 664-674 |
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| BBa_K3039019 | Ancestral PETase 3
This is the sequence of one of the four reconstructed ancestors of PETase with a His tag attached to it. The sequence has been obtained through the method of ancestral reconstruction. The His-tag was added to allow for conformation of expression and subsequent purification. |
S F Altschul, W Gish, W Miller, E W Myers, D J Lipman; Basic local alignment search tool (1990) J. Mol. Biol. 215, 403-410.
Keiko Watanabe, Takatoshi Ohkuri, Shinichi Yokobori, Akihiko Yamagishi; Designing Thermostable Proteins: Ancestral Mutants of 3-Isopropylmalate Dehydrogenase Designed by using a Phylogenetic Tree (2006) J. Mol. Biol. 355(4), 664-674 |
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| BBa_K3039020 | Ancestral PETase 4
This is the sequence of one of the four reconstructed ancestors of PETase with a His tag attached to it. The sequence has been obtained through the method of ancestral reconstruction. The His-tag was added to allow for conformation of expression and subsequent purification. |
S F Altschul, W Gish, W Miller, E W Myers, D J Lipman; Basic local alignment search tool (1990) J. Mol. Biol. 215, 403-410.
Keiko Watanabe, Takatoshi Ohkuri, Shinichi Yokobori, Akihiko Yamagishi; Designing Thermostable Proteins: Ancestral Mutants of 3-Isopropylmalate Dehydrogenase Designed by using a Phylogenetic Tree (2006) J. Mol. Biol. 355(4), 664-674 |
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| BBa_I746909 | T7 Promoter Characterisation
The Exeter iGEM characterisation of the Cambridge 2008 superfolder GFP driven by T7 promoter as part of the Bronze Medal Criteria. |
R Y Tsein; The Green Fluorescent Protein (1998) Annu. Rev. Biochem. 67, 509-544
F W Studier, A H Rosenberg, J J Dunn, J W Dubendorff; Use of T7 RNA polymerase to direct expression of cloned genes (1990) Meth. Enzymol. 185, 60–89. |
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| BBa_K2010000 | Wild Type PETase
The Exeter iGEM characterisation of E. coli K12 optimized DNA sequence for PETase submitted by Harvard BioDesign in 2016 as part of the Gold Medal Criteria. This part includes a T7 promoter (BBa_I712074), RBS 34 (BBa_B0034), and PETase fused with a His-tag, for purification |
Shosuke Yoshida, Kazumi Hiraga, Toshihiko Takehana, Ikuo Taniguchi, Hironao Yamaji, Yasuhito Maeda, Kiyotsuna Toyohara, Kenji Miyamoto, Yoshiharu Kimura, Kohei Oda, A bacterium that degrades and assimilates poly(ethylene terephthalate) (2016) Science 351(6278), 1196-1199 | ||
| Click the part number to be taken to the registry page. | ||||
