Difference between revisions of "Part:BBa K515000"
Line 3: Line 3:
 
<html>
 
<html>
 
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>
 
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>
−
<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>
+
<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>
 
</html>
 
</html>
  

Revision as of 21:26, 18 September 2011

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]


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