Difference between revisions of "Part:BBa K4613014"
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T3(BBa_K4613011) and C3(BBa_K4613012) could form protein complexes by elastin-like polypeptides(ELPs) monomers containing SpyTags and SpyCatchers. If you want to learn about the detailed introduction of T3 and C3, you can click the link below. https://parts.igem.org/Part:BBa_K4164011 https://parts.igem.org/Part:BBa_K4164012 | T3(BBa_K4613011) and C3(BBa_K4613012) could form protein complexes by elastin-like polypeptides(ELPs) monomers containing SpyTags and SpyCatchers. If you want to learn about the detailed introduction of T3 and C3, you can click the link below. https://parts.igem.org/Part:BBa_K4164011 https://parts.igem.org/Part:BBa_K4164012 | ||
Different functional proteins can be incorporated into the polymeric scaffolds in a flexible manner due to its programmability. In this part, NAU-CHINA 2023 incorporated ADH3, which is the most efficient OTA-detoxifying enzyme reported thus far and can hydrolyze OTA to nontoxic ochratoxin α(OTα) and L-β-phenylalanine(Phe). Moreover, its soluble protein expression of ADH3 in Escherichia coli has been realized. We fused ADH3 into T3 to immobilize the enzyme and increase the stability and sustainable production of ADH3. | Different functional proteins can be incorporated into the polymeric scaffolds in a flexible manner due to its programmability. In this part, NAU-CHINA 2023 incorporated ADH3, which is the most efficient OTA-detoxifying enzyme reported thus far and can hydrolyze OTA to nontoxic ochratoxin α(OTα) and L-β-phenylalanine(Phe). Moreover, its soluble protein expression of ADH3 in Escherichia coli has been realized. We fused ADH3 into T3 to immobilize the enzyme and increase the stability and sustainable production of ADH3. | ||
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+ | ==== Reference ==== | ||
+ | #Dai Z, Yang X, Wu F, et al.Living fabrication of functional semi-interpenetrating polymeric materials[J].Nat Commun,2021, 12 (1): 3422. | ||
+ | #Zakeri B, Fierer J O, Celik E, et al.Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin[J].Proc Natl Acad Sci U S A,2012, 109 (12): E690-7. | ||
+ | #Reddington S C, Howarth M.Secrets of a covalent interaction for biomaterials and biotechnology: SpyTag and SpyCatcher[J].Curr Opin Chem Biol,2015, 29: 94-9. | ||
+ | #Dai L, Niu D, Huang J W, et al.Cryo-EM structure and rational engineering of a superefficient ochratoxin A-detoxifying amidohydrolase[J].J Hazard Mater,2023, 458: 131836. | ||
Revision as of 03:09, 9 October 2023
T3-ADH3
T3(BBa_K4613011) and C3(BBa_K4613012) could form protein complexes by elastin-like polypeptides(ELPs) monomers containing SpyTags and SpyCatchers. If you want to learn about the detailed introduction of T3 and C3, you can click the link below. https://parts.igem.org/Part:BBa_K4164011 https://parts.igem.org/Part:BBa_K4164012 Different functional proteins can be incorporated into the polymeric scaffolds in a flexible manner due to its programmability. In this part, NAU-CHINA 2023 incorporated ADH3, which is the most efficient OTA-detoxifying enzyme reported thus far and can hydrolyze OTA to nontoxic ochratoxin α(OTα) and L-β-phenylalanine(Phe). Moreover, its soluble protein expression of ADH3 in Escherichia coli has been realized. We fused ADH3 into T3 to immobilize the enzyme and increase the stability and sustainable production of ADH3.
Reference
- Dai Z, Yang X, Wu F, et al.Living fabrication of functional semi-interpenetrating polymeric materials[J].Nat Commun,2021, 12 (1): 3422.
- Zakeri B, Fierer J O, Celik E, et al.Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin[J].Proc Natl Acad Sci U S A,2012, 109 (12): E690-7.
- Reddington S C, Howarth M.Secrets of a covalent interaction for biomaterials and biotechnology: SpyTag and SpyCatcher[J].Curr Opin Chem Biol,2015, 29: 94-9.
- Dai L, Niu D, Huang J W, et al.Cryo-EM structure and rational engineering of a superefficient ochratoxin A-detoxifying amidohydrolase[J].J Hazard Mater,2023, 458: 131836.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 940
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 1675
Illegal AgeI site found at 1363
Illegal AgeI site found at 1525 - 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 8