While authors often emphasize the few enzymes that have the most remarkable catalytic rates, this survery of enzymes has led to the author's appreciation of some important, general conclusions:
1. Most enzymes are not exceptionally fast; they are always good enough for their specific catalytic step.
2. Although enzymes could always be much faster if they changed so as to bind their substrates more weakly, actual enzymes must be able to discriminate in favor of their special substrate, and therefore they have sacrificed speed to obtain better binding. This means that specific control of individual metabolic steps is more important than overall speed.
3. Results for many hundreds of enzymes establish that a lower limit for a normal catalytic activity is1 s-1. Most enzymes have a catalytic rate between 10 and 300 s-1.
4. Allosteric regulation always results in a chance in the enzymes's affinity for its substrate. Even V-type enzymes (named for their large chance in catalytic velocity) always have a corresponding change in affinity for their substrate.
Thomas Traut has a PhD in molecular biology and has studied enzymes since 1974. As a professor at the University of North Carolina at Chapel Hill, he has focused on enzyme regulation and taught advanced enzymology to graduate students. Important findings from his research helped to define the mechanism of allosteric control for dissociating enzymes.
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