Difference between revisions of "Part:BBa K2992008"

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===Usage and Biology===
 
===Usage and Biology===
Thiolases are core metabolic enzymes involved in the melavonate pathway responsible for the conversion of acetyl-CoA to acetoacetyl-CoA. Results from our genome scale modeling suggested that exogenous thiolase was required for the production of acetone in our chosen volatile reporter organism <i>C. sporogenes.  Thiolase was therefore included in our acetone production pathway constructs in order to a volatile reporter for the prediction of botulinum toxin production following food manufacturing processes</i>. <br><br>
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Thiolases are core metabolic enzymes involved in the melavonate pathway responsible for the conversion of acetyl-CoA to acetoacetyl-CoA. Results from our genome scale modeling suggested that exogenous thiolase was required for the production of acetone in our chosen volatile reporter organism <i>C. sporogenes</i>.  Thiolase was therefore included in our acetone production pathway constructs in order to a volatile reporter for the prediction of botulinum toxin production following food manufacturing processes. <br><br>
 
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===Characterisation===
 
===Characterisation===
Data incoming. <br><br>
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This basic part was used as a composite in [https://parts.igem.org/wiki/index.php?title=Part:BBa_K2992028 BBa_K2992028], [https://parts.igem.org/wiki/index.php?title=Part:BBa_K2992029 BBa_K2992029], [https://parts.igem.org/wiki/index.php?title=Part:BBa_K2992030 BBa_K2992030], [https://parts.igem.org/wiki/index.php?title=Part:BBa_K2992034 BBa_K2992034], [https://parts.igem.org/wiki/index.php?title=Part:BBa_K2992035 BBa_K2992035], [https://parts.igem.org/wiki/index.php?title=Part:BBa_K2992036 BBa_K2992036]. This was then characterised using fluorescent assay, the results of which are shown below. See the [https://2019.igem.org/Team:Nottingham/Results results page] for more information. 
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<br> [[File:Acetone data.png]]
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<partinfo>BBa_K2992008 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K2992008 SequenceAndFeatures</partinfo>
  
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===References===
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Dennis P. Wiesenborn, E. (1988). Thiolase from Clostridium acetobutylicum ATCC 824 and Its Role in the Synthesis of Acids and Solvents. Applied and Environmental Microbiology, [online] 54(11), p.2717. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC204361/ [Accessed 21 Oct. 2019].
  
===References===
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Incoming.
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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K2992008 parameters</partinfo>
 
<partinfo>BBa_K2992008 parameters</partinfo>
 
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Latest revision as of 00:49, 22 October 2019


Thiolase gene thl from C. acetobutylicum.

The thiolase gene encodes an acetyl-coenzyme A acetyltransferases from C. acetobutylicum.


Usage and Biology

Thiolases are core metabolic enzymes involved in the melavonate pathway responsible for the conversion of acetyl-CoA to acetoacetyl-CoA. Results from our genome scale modeling suggested that exogenous thiolase was required for the production of acetone in our chosen volatile reporter organism C. sporogenes. Thiolase was therefore included in our acetone production pathway constructs in order to a volatile reporter for the prediction of botulinum toxin production following food manufacturing processes.

Characterisation

This basic part was used as a composite in BBa_K2992028, BBa_K2992029, BBa_K2992030, BBa_K2992034, BBa_K2992035, BBa_K2992036. This was then characterised using fluorescent assay, the results of which are shown below. See the results page for more information.
Acetone data.png

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal XbaI site found at 355
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal XbaI site found at 355
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal XbaI site found at 355
  • 1000
    COMPATIBLE WITH RFC[1000]

References

Dennis P. Wiesenborn, E. (1988). Thiolase from Clostridium acetobutylicum ATCC 824 and Its Role in the Synthesis of Acids and Solvents. Applied and Environmental Microbiology, [online] 54(11), p.2717. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC204361/ [Accessed 21 Oct. 2019].