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Enzymes can accelerate reactions in several ways, all of which lower the [[activation energy]] (ΔG<sup>‡</sup>, [[Gibbs free energy]])
# By stabilizing the transition state:
#* Creating an environment with a charge distribution complementary to that of the transition state to lower its energy
# By providing an alternative reaction pathway:
#* Temporarily reacting with the substrate, forming a covalent intermediate to provide a lower energy transition state
# By destabilising the substrate ground state:
#* Distorting bound substrate(s) into their transition state form to reduce the energy required to reach the transition state
#* By orienting the substrates into a productive arrangement to reduce the reaction [[entropy]] change (the contribution of this mechanism to catalysis is relatively small)
Enzymes may use several of these mechanisms simultaneously. For example, [[protease]]s such as [[trypsin]] perform covalent catalysis using a [[catalytic triad]], stabilise charge build-up on the transition states using an [[oxyanion hole]], complete [[hydrolysis]] using an oriented water substrate.

Translations:Enzyme/35/en - Revision history

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