Difference between revisions of "Part:BBa K2570009"

Revision as of 02:02, 16 October 2018

Degrading enzyme complex：araC＋atoD＋atoA＋adhE2

This year, our team aims to tackle environmental problems in daily lives. We focused on harmful bacteria and unpleasant smell under the armpits. From the literature of Andreas Natsch, we knew about that the odorant acid E-3-methyl-2-hexenoicacid (E-3M2H) is abundant and quantitatively dominant human odorant. [1] Therefore, we tried to eliminate such unpleasant axilla odors in an innovative method by degrading the odorant acid. Referring to potential production platform of n-butanol in E. coli [2], we designed a combined part to degrade E-3-methyl-2-hexenoicacid (E-3M2H).

This is a combined part of BBa_K2570006, BBa_K2570007 and BBa_K2570008 degrading main unpleasant axilla odors E-3M2H(E-3-methyl-3-hexenoic acid). This gene cluster expresses three enzymes, of which atoD and atoA from E.coli and adhE2 from Clostridium acetobutylicum ATCC 824. The function of atoDA mediates reductive conversion of 3-methyl 2-hexenoic acid to 3-methyl-2-acetyl-CoA with acetyl-CoA as the CoA donor, for fatty acid activation and its subsequent degradation. [2] AdhE2 catalyzes reduction of 3-methyl-2-acetyl-CoA to 3-methyl 2-hexenol at the expense of NADH. [3]

Fig.1 Possible pathway of degrading the odorant acid E-3M2H.

In our design, the cluster includes an arabinose promoter, strong RBS, atoDA coding region, and adhE2 coding region. atoDA and adhE2 are expressed under the induction of arabinose to achieve degradation of the odorant acid.

Fig2. Circuit of degrading the odorant acid E-3M2H.

Sequence and Features