Difference between revisions of "Part:BBa K2588016"

 
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<p>kivD is originally derived from <i>lactococcus lactis</i> and codes for alpha-ketoisovalerate decarboxylase, which catalyzes the reaction of 2-ketoisovcarproate to 3-methyl-1-butane as the last step of a pathway, engineered by Connor et al for enhanced 3-methyl-1-butanole-synthesis in <i>E.coli</i>.<sup>1,2</sup></p>
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<p>kivD is originally derived from <i>lactococcus lactis</i> and codes for alpha-ketoisovalerate decarboxylase, which catalyzes the reaction of 2-ketoisocaproate to 3-methyl-1-butane as the last step of a pathway, engineered by Connor et al for enhanced 3-methyl-1-butanole-synthesis in <i>E.coli</i>.<sup>1,2</sup></p>
  
 
<h2>Usage and Biology</h2>
 
<h2>Usage and Biology</h2>

Latest revision as of 02:28, 18 October 2018


Alpha-ketoisovalerate decarboxilase from Lactococcus Lactis

kivD is originally derived from lactococcus lactis and codes for alpha-ketoisovalerate decarboxylase, which catalyzes the reaction of 2-ketoisocaproate to 3-methyl-1-butane as the last step of a pathway, engineered by Connor et al for enhanced 3-methyl-1-butanole-synthesis in E.coli.1,2

Usage and Biology

We used kivD in our project, as part of our 3-methyl-1-butane module, BBa_K2588024, which is intended to modify E.coli for the production of the lure 3-methyl-1-butanol from pyruvate.

References

  1. Connor, M. R. & Liao, J. C. Engineering of an Escherichia coli strain for the production of 3-methyl-1-butanol. Appl. Environ. Microbiol. (2008). doi:10.1128/AEM.00468-08
  2. Connor, M. R., Cann, A. F. & Liao, J. C. 3-Methyl-1-butanol production in Escherichia coli: random mutagenesis and two-phase fermentation. Appl. Microbiol. Biotechnol. 86, 1155–1164 (2010).

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
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1111