Difference between revisions of "Part:BBa K1604019"

Revision as of 22:51, 17 September 2015

RBS + β-carotene 15,15'-dioxygenase (blh gene)

This part contains a strong RBS and the blh gene. β-carotene 15,15’-dioxygenase is involved in retinal biosynthesis and catalizes the last step of the pathway by cleaving one molecule of β-carotene into two molecules of retinal.

Usage and Biology

Blh is the gene that encodes for this enzyme, and was first isolated in the uncultured bacteria SAR86 [1] . Blh is present in other organisms (i.e. cyanobacteria and algae) however enzymes involved in the cleavage of β-carotene that involve different mechanisms are found in many other organisms.

The enzyme requires oxygen for the cleavage of β-carotene, which was demonstrated to be provided by water [2] . This data are consistent with the fact the bacteria lives in deep marine waters. It requires Fe²⁺ that is coordinated by 4 His residues that are highly conserved.

We placed BBa_K1604019 under a costituve promoter and we characterized blh.
To see the characterization results check the part BBa_K1604021 and the part BBa_K1604022

Check out our Wiki UNITN-Trento iGEM 2015!

Martinez A.,"Proteorhodopsin Photosystem Gene Expression Enables Photophosphorylation in a Heterologous Host" Proceedings of the National Academy of Sciences 104.13 (2007): 5590-595. Web
Yeong-Su Kim, Retinal production from b-carotene by b-carotene 15,15'-dioxygenase from an unculturable marine bacterium, Biotechnol Lett (2010) 32:957–961

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 NgoMIV site found at 202
1000
COMPATIBLE WITH RFC[1000]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K1604019 short</partinfo>
-This part contains RBS and blh gene. &#946;-carotene 15,15&rsquo;-dioxygenase is involved in retinal biosynthesis and catalizes the last step of the  pathway by cleaving one molecule of &#946;-carotene into two molecules of retinal.  Blh is the gene that encodes for this enzyme, and was first isolated in the uncultured bacteria SAR86 <html><a href="#fn:1" id="fnref:1" title="see footnote" class="footnote">[1]</a></html> . Blh is present in other organisms (i.e. cyanobacteria and algae) however enzymes involved in the cleavage of &#946;-carotene that involve different mechanisms are found in many other organisms.
+This part contains a strong RBS and the blh gene. &#946;-carotene 15,15&rsquo;-dioxygenase is involved in retinal biosynthesis and catalizes the last step of the  pathway by cleaving one molecule of &#946;-carotene into two molecules of retinal.
+===Usage and Biology===
+Blh is the gene that encodes for this enzyme, and was first isolated in the uncultured bacteria SAR86 <html><a href="#fn:1" id="fnref:1" title="see footnote" class="footnote">[1]</a></html> . Blh is present in other organisms (i.e. cyanobacteria and algae) however enzymes involved in the cleavage of &#946;-carotene that involve different mechanisms are found in many other organisms.
 The enzyme requires oxygen for the cleavage of &#946;-carotene, which was demonstrated to be provided by water <html><a href="#fn:2" id="fnref:2" title="see footnote" class="footnote">[2]</a></html> . This data are consistent with the fact the bacteria lives in deep marine waters. It requires Fe<sup>2+</sup> that is coordinated by 4 His residues that are highly conserved.
-===Usage and Biology===
 We placed BBa_K1604019 under a costituve promoter and we characterized blh. <br>
 To see the characterization results check the part <html><a href="https://parts.igem.org/Part:BBa_K1604021#Usage_and_Biology">BBa_K1604021</a></html> and the part <html><a href="https://parts.igem.org/wiki/index.php?title=Part:BBa_K1604022">BBa_K1604022</a></html>