Catalytic selectivity concerns which reaction products form when competing reaction mechanisms are available. Faster conversion is valuable when a process would otherwise be impractically slow; a suitable catalyst can also favour a useful product within the available time. In an illustrative pair of irreversible first-order reactions A to B and A to D, the initial fraction of converted A going to B is . Multiplying both rate constants by the same factor changes speed but leaves this fraction unchanged; changing their relative values changes the kinetic product split. This is a finite-time kinetic illustration, not a new equilibrium constant.
A catalyst need not accelerate every competing chemical reaction equally. Enzymes, for example, can distinguish substrates through their active sites.[ref]
Chemistry 2e by Paul Flowers and others. §12.7, Enzyme Structure and Function, Figure 12.25: substrate binding and specificity
If every relevant reversible channel eventually equilibrates in a closed system, its final chemical equilibrium still obeys the endpoint thermodynamics. Selective acceleration, product removal, or external driving can make an observed product distribution depend on time and operating conditions. A claim of improved yield must specify those conditions. Articles by others on the same topic
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