It is well known that enzymes seldom act completely independently, yet I am struggling to find a good example of a model system where:
1) The monomer is active (unlike Isocitrate dehydrogenase where both units contribute to a shared active site)
2) The hetero-dimer has a different activity but is still active (excluding complexes like Trypsin:BPTI)
3) The enzyme activity is easy to monitor and quantify (excluding DNA polymerases /transcription factors)
4) the enzyme would be soluble and active when expressed recombinantly in E.coli
I would be very thankful for any suggestions, or even just better keywords for my litterature searches.
I'm not sure but I think some alpha-helical coiled-coil heterodimers might fit your criteria.
I memory serves me, I think either the E. coli trpED or trpBA gene products might do what you want, each pair is a heterdimer but can act independently as well.
Dear Bjarte
Cu,Zn Sod1 could be a possible target..
You can produce in E.coli the WT heterodimer or the monomeric F50E/G51E/E133Q monomeric mutantArticle Synthesis and Characterization of a Monomeric Mutant Cu/Zn S...
Both dimeric and monomeric forms where extensivelly characterized in terms of structure and activity.
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