Enzymes catalyze all the reactions of life. They're what allow you to extract materials and energy from your environment and turn that into muscle and tissue and fat. That's all done by enzymes. They're pretty remarkable chemists - they're even better than Caltech chemists.
No human can design a good enzyme, yet we are surrounded by them after 3.5 billion years of work by evolution.
Enzymes are masters of chemistry. They evolved over billions of years to perform specific biological functions. They make complex materials with virtually no waste.
It was obvious-to me at any rate-that the answer was to why an enzyme is able to speed up a chemical reaction by as much as 10 million times. It had to do this by lowering the energy of activation-the energy of forming the activated complex. It could do this by forming strong bonds with the activated complex, but only weak bonds with the reactants or products.
The detailed geometry of the coenzyme molecule as a whole is fascinating in its complexity.
Looking back on my 50-year eclectic journey in research, I am grateful that it has gone as well as it has, although still not clever enough to open the black box of enzyme structure.
As has repeatedly been stated, the underlying hypothesis, which in a number of cases has been supported by direct experimental evidence, is that each gene controls the production, function, and specificity of a particular enzyme.
All these bacteria that coat our skin and live in our intestines, they fend off bad bacteria. They protect us. And you can't even digest your food without the bacteria that are in your gut. They have enzymes and proteins that allow you to metabolize foods you eat.
There are enzymes called restriction enzymes that actually digest DNA.
So many of the chemical reactions occurring in living systems have been shown to be catalytic processes occurring isothermally on the surface of specific proteins, referred to as enzymes, that it seems fairly safe to assume that all are of this nature and that the proteins are the necessary basis for carrying out the processes that we call life.
Life does depend on accurate replication of molecules, and its complexity often requires that an enzyme shall accept one molecular species or type and transform it to equally specific products.
I began my thesis research at Harvard by working with a team in the laboratory of William N. Lipscomb, a Nobel chemistry Laureate, in 1976, on the structure of carboxypeptidase A. I did postdoctoral studies with David Blow at the MRC lab of Molecular Biology in Cambridge studying chymotrypsin.
