Difference between revisions of "Part:BBa K4673021"

 
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<partinfo>BBa_K4673021 short</partinfo>
 
<partinfo>BBa_K4673021 short</partinfo>
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The fadH operator is the fadR binding site that encodes 2,4-dienoyl-CoA reductase, an auxiliary ß-oxidation enzyme. It is responsible for reducing the cis-2-alkenoyl-CoA formed by ß-oxidation of unsaturated fatty acids having double bonds at even-numbered carbon atoms. On the DNA sequences, the putative FadR binding site overlaps the transcriptional start site and the downstream ArcA binding site. Based on the position of the putative FadR binding site, it appears that both FadR and ArcA negatively regulate fadH expression, while CRP activates fadH transcription (Cho et al., 2006).
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In addition, the oleate induction of fadH was similar to the induction observed for fadBA, which encodes the enzyme complex responsible for the majority of the degradation cycle. In contrast, the induction of fadH was stronger compared to that of fadM, which codes for an additional auxiliary enzyme (Feng et al., 2010).
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As a key component of our team’s project, we modified the pET-22b-LK vector and replaced the LacO to the fadH operator that is cloned in front of the Lumbrokinase gene, thereby enabling us to carry out the oleate induction. The fadH operator enhances our project’s prospect for success as it plays an important role in the binding of fadR, a fatty acid metabolism regulator protein that functions as a switch regulating the expression of the target protein(Lumbrokinase).
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The source of the part:
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The FadH gene was composited during the experimental procedures by team Taipei_KCISLK_V1 in the lab with the reference of several papers.
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The fadH operator is the fadR binding site that encodes 2,4-dienoyl-CoA reductase, an auxiliary b-oxidation enzyme. It is responsible for reducing the cis-2-alkenoyl-CoA formed by b-oxidation of unsaturated fatty acids having double bonds at even-numbered carbon atoms.
 
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Revision as of 15:50, 9 October 2023


FadH operator The fadH operator is the fadR binding site that encodes 2,4-dienoyl-CoA reductase, an auxiliary ß-oxidation enzyme. It is responsible for reducing the cis-2-alkenoyl-CoA formed by ß-oxidation of unsaturated fatty acids having double bonds at even-numbered carbon atoms. On the DNA sequences, the putative FadR binding site overlaps the transcriptional start site and the downstream ArcA binding site. Based on the position of the putative FadR binding site, it appears that both FadR and ArcA negatively regulate fadH expression, while CRP activates fadH transcription (Cho et al., 2006).


In addition, the oleate induction of fadH was similar to the induction observed for fadBA, which encodes the enzyme complex responsible for the majority of the degradation cycle. In contrast, the induction of fadH was stronger compared to that of fadM, which codes for an additional auxiliary enzyme (Feng et al., 2010).


As a key component of our team’s project, we modified the pET-22b-LK vector and replaced the LacO to the fadH operator that is cloned in front of the Lumbrokinase gene, thereby enabling us to carry out the oleate induction. The fadH operator enhances our project’s prospect for success as it plays an important role in the binding of fadR, a fatty acid metabolism regulator protein that functions as a switch regulating the expression of the target protein(Lumbrokinase).


The source of the part: The FadH gene was composited during the experimental procedures by team Taipei_KCISLK_V1 in the lab with the reference of several papers.



Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]