Part:BBa_K3747015
pMMO-m1
Particulate methane monooxygenase m1 mimic. pMMO-m1 is described in Kim et al 2019 [1]. In this paper active pMMO is shown using a scaffold and additional reductant duroquinol. The authors express several pMMO constructs on a high copy number plasmid under control of a T7 promotor with a lac operator. In this paper the authors construct several pMMO mimics and they measure methanol production. They construct mimics pMMO-m1 to m4, which all contain pmmoB1 and –B2 substructures either linked in series or parallel to an apo form of human heavy-chain ferritin (huHF), which works as a scaffold. This to mimic the active site in native particulate MMO, but in a soluble form.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 377
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 377
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 377
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 377
Illegal NgoMIV site found at 1008
Illegal NgoMIV site found at 1043 - 1000COMPATIBLE WITH RFC[1000]
[1] Kim, H.J., Huh, J., Kwon, Y.W. et al. Biological conversion of methane to methanol through genetic reassembly of native catalytic domains. Nat Catal 2, 342–353 (2019). https://doi.org/10.1038/s41929-019-0255-1
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