Difference between revisions of "Part:BBa K515000"

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.

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K515000 short</partinfo>
+<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.[1] There are several different pathways to produce indole-3-acetic acid. [2] We are using genes from the IAM pathway (IaaM and IaaH) of the plant pathogen, <i>Psuedomonas savastanoi</i> to produce indole-3-acetic acid in <i>E. coli</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> tryptophan --> indole acetamide --> indole-3-acetic acid </p>
+</html>
 <!-- Add more about the biology of this part here
@@ Line 19: / Line 18: @@
 <partinfo>BBa_K515000 parameters</partinfo>
 <!-- -->
+<html>
+<p><b>This BioBrick has been sequence verified.</b></p>
+<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>
 <h2>References</h2>
-[1]http://ecocyc.org/META/NEW-IMAGE?type=GENE&object=G-5821
+<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>
-[2]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>
+</html>
+==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.