Difference between revisions of "Part:BBa K515000"
 
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<partinfo>BBa_K515000 short</partinfo>
 
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IAA tryptophan monooxygenase catalyzes the oxidative carboxylation of L-tryptophan to indole-3-acetamide. The enzymes of the IAM pathway (IaaM and IaaH) originate from the plant pathogen, <i>Psuedomonas savastanoi</i> which produces and secretes indole-3-acetic acid (auxin).
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IAA tryptophan monooxygenase (IaaM) catalyzes the oxidative carboxylation of L-tryptophan to indole-3-acetamide which acts as an intermediate to the production of indole-3-acetic acid in the IAM pathway. This auxin producing pathway originates from the plant pathogen, <i> Pseudomonas savastanoi </i> </p>
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<p>This is one of the parts of our composite auxin expressing construct, <a href="https://parts.igem.org/wiki/index.php?title=Part:BBa_K515100" target="_blank">BBa_K515100</a>.</p>
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The sequence has been codon optimised for <i>E. coli</i> and <i>B. subtilis</i> and is under control of the pVEG promoter with an RBS also suitable for <i>E. coli</i> and <i>B. subtilis</i>.
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<partinfo>BBa_K515000 parameters</partinfo>
 
<partinfo>BBa_K515000 parameters</partinfo>
 
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<p><b>This BioBrick has been sequence verified.</b></p>
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<p><b>For the full characterisation of the device, please refer to the <a href="https://parts.igem.org/wiki/index.php?title=Part:BBa_K515100"><b>BBa_K515100</b></a> page.</b>
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<h2>References</h2>
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<p>[1]Spaepen S. et al., 2007. Indole-3-acetic acid in microbial and microorganism-plant signaling. <i>Federation of European Microbiological Societies Microbiology Reviews </i>, 31, pp.425–448 </p>
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==Contribution: NUDT_CHINA 2015==
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Author: Xinyuan Qiu
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Summary: We built a new part based on this part to extend its function.
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We designed a new part by removing the RBS from this part to extend its usage.
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====A new Bio-brick was designed based on this part====
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Primers used to build the new part:
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F-Prime: 5’- GGAATTCGCGGCCGCTTCTAGAGATGTTTGGACCGG-3’
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R-Prime: 5’- GCGGCGGACTAGTCTTATTAGTCCCCCAGCG -3’
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For further information,
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See BBa_K1789000
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This part was sent to the registry.

Latest revision as of 16:35, 18 September 2015

IaaM - tryptophan-2-mono-oxygenase IAA tryptophan monooxygenase (IaaM) catalyzes the oxidative carboxylation of L-tryptophan to indole-3-acetamide which acts as an intermediate to the production of indole-3-acetic acid in the IAM pathway. This auxin producing pathway originates from the plant pathogen, Pseudomonas savastanoi

This is one of the parts of our composite auxin expressing construct, BBa_K515100.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 450
    Illegal BamHI site found at 1395
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 157
  • 1000
    COMPATIBLE WITH RFC[1000]


This BioBrick has been sequence verified.

For the full characterisation of the device, please refer to the BBa_K515100 page.

References

[1]Spaepen S. et al., 2007. Indole-3-acetic acid in microbial and microorganism-plant signaling. Federation of European Microbiological Societies Microbiology Reviews , 31, pp.425–448


Contribution: NUDT_CHINA 2015

Author: Xinyuan Qiu

Summary: We built a new part based on this part to extend its function.

We designed a new part by removing the RBS from this part to extend its usage.

A new Bio-brick was designed based on this part

Primers used to build the new part:

F-Prime: 5’- GGAATTCGCGGCCGCTTCTAGAGATGTTTGGACCGG-3’

R-Prime: 5’- GCGGCGGACTAGTCTTATTAGTCCCCCAGCG -3’


For further information,

See BBa_K1789000

This part was sent to the registry.