My apologies for the utter lack of posting over the past week. I’ve got stuff sitting around waiting to be written about, and I just haven’t been writing. I’m not going to make excuses; I just haven’t been managing my time well. While you wait for me to post again (soon, I promise), I give you this article on “intelligently designing” promiscuous enzymes to perform specific functions. Here’s a quote from the write up:
According to the theory of divergent molecular evolution, primordial enzymes and other proteins started out as “promiscuous” so that primitive organisms would be better able to adapt to their environment. Driven by selective pressures, these promiscuous enzymes and other proteins evolved along divergent lines to acquire the specialized functions needed by a host organism to survive.
The Berkeley researchers identified the plasticity residues for the Grand fir sesquiterpene synthase, then systematically recombined mutations of these residues through site-directed mutagenesis, based on a mathematical model developed by Yoshikuni. Construction of the seven sesquiterpene synthases was accomplished with the screening of fewer than 2,500 mutants. An alterative approach, called directed evolution or molecular breeding, that is currently being tested at other laboratories, requires the screening of tens of thousands to a million or more mutants.
I wonder if this is how the Flying Spaghetti Monster works its magic.