Difference between revisions of "Part:BBa K590034"

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<partinfo>BBa_K590034 short</partinfo>
 
<partinfo>BBa_K590034 short</partinfo>
  
This part encodes FabH2. [http://2011.igem.org/Team:Washington 2011 University of Washington iGEM Team] has attempted to produce branched alkanes using this part and the [https://parts.igem.org/wiki/index.php?title=Part:BBa_K590025 Petrobrick].  
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This part encodes FabH2. [http://2011.igem.org/Team:Washington 2011 University of Washington iGEM Team] has produced  even chain length  alkanes using this part and the [https://parts.igem.org/wiki/index.php?title=Part:BBa_K590025 Petrobrick]. In addition, expression of this part and the [https://parts.igem.org/wiki/index.php?title=Part:BBa_K590025 Petrobrick] should theoretically produce branched chain alkanes, but we have not been able to demonstrate this effect, possibly due to the absence of the appropriate substrates in ''E. coli''
  
 
===Usage and Biology===
 
===Usage and Biology===
  
FabH2 is from ''Bacillus subtilis''. The FabH family of proteins initiates fatty acid elongation by converting an Acyl-CoA into an Acyl-ACP, with is extended by 2 carbon units to form longer chain length fatty acids. Normally, FabH proteins use a simple 2-carbon acetyl-CoA to start fatty acid biosynthesis, resulting in linear fatty acids. However, FabH2 can also use Isobutyryl-CoA, Isovaleryl-CoA, and 2-Methylbutyryl-CoA (products from Valine, Leucine, and Isoleucine degredation, resulting in 2-methyl branched fatty acid production.  
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FabH2 is from ''Bacillus subtilis''. The FabH family of proteins initiates fatty acid elongation by converting an Acyl-CoA into an Acyl-ACP, with is extended by 2 carbon units to form longer chain length fatty acids. Normally, FabH proteins use a simple 2-carbon acetyl-CoA to start fatty acid biosynthesis, resulting in linear fatty acids. However, FabH2 can also use Isobutyryl-CoA, Isovaleryl-CoA, and 2-Methylbutyryl-CoA (products from Valine, Leucine, and Isoleucine degredation), resulting in 2-methyl branched fatty acid production. In addition, FabH2  has been hypothesized to start fatty acid elongation with a straight 3-carbon unit(propionyl-CoA), yielding odd chain length fatty acids, which could be converted into even chain length alkanes by the[https://parts.igem.org/wiki/index.php?title=Part:BBa_K590025 Petrobrick].Expression of FabH2 on the same plasmid as the PetroBrick( Part 
  
 
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Revision as of 17:36, 21 October 2011

FabH2

This part encodes FabH2. [http://2011.igem.org/Team:Washington 2011 University of Washington iGEM Team] has produced even chain length alkanes using this part and the Petrobrick. In addition, expression of this part and the Petrobrick should theoretically produce branched chain alkanes, but we have not been able to demonstrate this effect, possibly due to the absence of the appropriate substrates in E. coli

Usage and Biology

FabH2 is from Bacillus subtilis. The FabH family of proteins initiates fatty acid elongation by converting an Acyl-CoA into an Acyl-ACP, with is extended by 2 carbon units to form longer chain length fatty acids. Normally, FabH proteins use a simple 2-carbon acetyl-CoA to start fatty acid biosynthesis, resulting in linear fatty acids. However, FabH2 can also use Isobutyryl-CoA, Isovaleryl-CoA, and 2-Methylbutyryl-CoA (products from Valine, Leucine, and Isoleucine degredation), resulting in 2-methyl branched fatty acid production. In addition, FabH2 has been hypothesized to start fatty acid elongation with a straight 3-carbon unit(propionyl-CoA), yielding odd chain length fatty acids, which could be converted into even chain length alkanes by thePetrobrick.Expression of FabH2 on the same plasmid as the PetroBrick( Part

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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 310
    Illegal AgeI site found at 949
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 355