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- | + | <p>kivD is originally derived from <i>lactococcus lactis</i> and codes for alpha-ketoisovalerate decarboxylase, which catalyzes the reaction of 2-ketoisocarproate 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> | ||
Revision as of 02:23, 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-ketoisocarproate 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
- 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
- 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:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 1111